1 s2.0 S0963996924006458 Main

Food Research International 190 (2024) 114575
Contents lists available at ScienceDirect
Food Research International

journal homepage: www.elsevier.com/locate/foodres
Review
A comprehensive review on the recent trends in extractions, pretreatments

and modifications of plant-based proteins
Nevetha Ravindran , Sushil Kumar Singh , Poonam Singha *
Department of Food Process Engineering, National Institute of Technology Rourkela, India
A R T I C L E I N F O A B S T R A C T
Keywords: Plant-based proteins offer sustainable and nutritious alternatives to animal proteins with their techno-functional
Modifications attributes influencing product quality and designer food development. Due to the inherent complexities of plant
Nutrition proteins, proper extraction and modifications are vital for their effective utilization. This review highlights the
Plant protein
emerging sources of plant-based proteins, and the recent statistics of the techniques employed for pretreatment,
Protein functionality
extraction, and modifications. The pretreatment, extraction and modification approach to modify plant proteins
Seed proteins
Sustainable sources have been classified, addressed, and the recent applications of such methodologies are duly indicated.
Furthermore, this study furnishes novel perspectives regarding the potential impacts of emerging technologies on
the intricate dynamics of plant proteins. A thorough review of 100 articles (2018–2024) shows the researchers’
keen interest in investigating novel plant proteins and how they can be used; seeds being the main source for
protein extraction, followed by legumes. Use of by-products as a protein source is increasing rapidly, which is
noteworthy. Protein studies still lack knowledge on protein fraction, antinutrients, and pretreatments. The use of
physical methods and their combination with other techniques are increasing for effective and environmentally
friendly extraction and modification of plant proteins. Several studies explore the effect of protein changes on
their function and nutrition, especially with a goal of replacing ingredients with plant proteins that have
improved or enhanced qualities. However, the next step is to investigate the sophisticated modification methods
for deeper insights into food safety and toxicity.
1. Introduction vegan products. Protein is a basic human global need, and all the above
factors associated with protein-based products strongly impact con
Proteins are the building blocks of every living organism, making sumer preferences. A study conducted by Onwezen et al. (2021) on
them an essential nutrient. The UN Food and Agriculture Organization alternative protein acceptance revealed that familiarity, taste, health
predicted that proteins will be the most deficient nutrient soon and preferences, disgust, food neophobia, attitudes, and social norms
stated that each human deserve well-suffice good quality protein impacted consumer opinions. Transitioning to the realm of alternative
(Arrutia et al., 2020). While animal-derived proteins are the most pre proteins, the sources can be categorized into plant-based proteins,
vailing choice in human protein consumption, daunting environmental cultured meat, insect proteins, and microbial proteins (algae and fungi).
issues (climate change and imbalanced ecosystem), health implications, Of all, plant-based proteins are highly accepted, followed by microbial
and pressing concerns of sustainability have shifted government policies proteins, cultured meat, and insect proteins.
and consumer preferences towards plant-based proteins (Sá et al., The greater demand in the plant protein market and the resulting
2020b). Additionally, the drawbacks of animal proteins, includes high strain on conventional crop sources is the key driver for extraction of
cost, cholesterol, inefficient feed conversion, antibiotic resistance, pan proteins from alternative plant sources. Confining this demand to the
demics, and cultural factors., In contrast plant proteins, offer lower food industry, it stems from the growing consumer consciousness and
microbial infestation risk, better malnutrition management, and awareness about the food they consume. The extraction process addi
increased significance of plant-based diets (Arrutia et al., 2020; Dash tionally facilitates the liberation of proteins from their associated com
et al., 2022). This shift is supported by the growing popularity of pounds, such as sugars, fatty acids, polyphenols, pigments, and
veganism and the modern shelves of supermarkets filled with attractive antinutrients, yielding proteins with a neutral color and flavor. In
* Corresponding author at: Department of Food Process Engineering, National Institute of Technology Rourkela, OD, India.
E-mail addresses: [email protected] (N. Ravindran), [email protected] (S. Kumar Singh), [email protected] (P. Singha).
https://doi.org/10.1016/j.foodres.2024.114575
Received 22 February 2024; Received in revised form 26 May 2024; Accepted 26 May 2024
Available online 28 May 2024
0963-9969/© 2024 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.
N. Ravindran et al. Food Research International 190 (2024) 114575
contrast to previous eras where proteins were primarily employed for Table 1
body building, they are now harnessed as functional constituents for Common proteins and their focus of interest.
transforming food texture and stability. Proteins have also become Protein Focus of interest Reference
instrumental in developing novel processed foods by: a) offering
Soy Excellent nutritional (all nine (Singh, 2016; Singha, 2017;
customized structures (eg: 3D food printing); b) developing meat and essential amino acids) and Zhang et al., 2015)
dairy substitutes, thereby expanding the options to consumers; c) miti functional properties
gating allergenic properties and d) isolation of enzymes and bioactive Pea High availability, versatility, (Colmenero, 2014; Pavani,
peptides for shelf life extension and other specialized purposes (Gopir nutritious and hypoallergenic; Singha, Rajamanickam, &
could be obtained from co- Singh, 2024; Pavani, Singha,
ajah, Singha, Javad, & Rizvi, 2020; Grossmann & Weiss, 2021). The product of pea starch extraction & Singh, 2024)
emerging sources and trends in alternative plant protein extraction and Rice Highly nutritious (equivalent to (Jayaprakash et al., 2022)
related modifications will tend to reduce the inherent protein allerge casein and soy protein),
nicity and commercial production stress from the existing animal pro hypoallergenic, and easily
digestible; high net protein
teins and conventional plant proteins, such as soybean, and pea.
utilization value among cereals
However, compared to animal proteins, plant proteins are typically Buckwheat High lysine content; high (Chrungoo et al., 2016)
considered nutritionally inadequate or inferior due to lack of certain biological value
essential amino acids and also the nutritional value of these protein Seeds Antioxidant, antihypertensive, (Dash, Singh, & Singha, 2024;
sources is highly dependent on their processing, bioavailability, amino antimicrobial, and antiviral; Sonawane, S.K., 2018)
high amino acid content; boosts
acid profile, purity, digestibility, and anti-nutritional factors (Sá et al., nutrition
2020b). Leaves RuBisCO (ribulose-1,5- (Pérez-Vila et al., 2022)
Research is being carried out to address these shortcomings and bisphosphate carboxylase/
improve the quality of plant proteins; the development of novel tech oxygenase) protein which has
better amino acid profile with
nologies and modifications in existing extraction and modification
high level of sulphur-containing
practices help in improving extraction yield, nutrition and functionality amino acids; yield good
of such protein sources and make them viable. Yet, there is a lack of functional properties; promotes
collective information of the statistical data on plant protein extraction sustainability
comprising the factors like pretreatments undergone before extraction, Biomass or Support sustainability; improve (Gorde, Dash, Singh, &
Industrial by- circular bio-economy Singha, 2024; Pavani, Singh,
extraction techniques and their transition phase, and indulgence of
products & Singha, 2024; Segatto,
novel modification methods. Therefore, this review focuses on exploring Stahl, Zanotti, & Zuin, 2022)
the existing and emerging plant-based proteins, over the timeline
2018–2024, accounting the above-mentioned factors and updating the
recent statistics of the techniques employed for pretreatment, extrac Dolichos lablab L., grass pea, mung bean, panda bean, yellow pea, black
tion, and modifications. The current trends on their extraction methods, turtle bean, seeds from album, bitter gourd, camelina oilseeds (Singh,
pretreatments for extraction and modifications (structural, functional, Rajpurohit, & Singha, 2021), flixweed, ginkgo, hemp, perilla, Sunn
and physicochemical) done for their betterment are reviewed. Based on hemp, manila tamarind, pomegranate, rice endosperm, wheat germ,
the review, recommendations are provided. Additionally, the impact of soursop and other sources like coconut, clove, and potato. The growing
protein modifications on their functionality and nutritional character demand for proteins shifted our focus to agricultural biomass and in
istics are discussed. dustrial by-products as well. Thus, proteins are extracted from bran
(rice, sesame), oilseed meals (amaranth, cottonseed, mustard, peanut,
2. Plant-based protein sources rapeseed, sesame) and soybean okra (residue after soymilk production);
these are gaining significance as it reduces waste generation and
Plant-based proteins are more sustainable choice than any other improve the economy.
alternative proteins as they provide a low-calorie diet with significantly
low-fat levels. They are a potential source of essential amino acids, vi 3. Extraction of protein from plant-based sources
tamins, and minerals for consumers allergic to animal proteins. In
addition to their nutritional content, the physicochemical, structural, 3.1. Overview
and behavioral properties of proteins, upon processing, play an essential
role in defining the final product quality. They are significant in deter Extraction of plant proteins involves four distinct stages: (i) cell
mining foam stability, viscosity, emulsification, gelation properties, disruption; (ii) protein solubilization; (iii) precipitation of proteins at
water/oil holding capacity, fat absorption, and food matrix stabilization their isoelectric point; and (iv) concentration or isolation of protein
(Dash, Singh, & Singha, 2024). (Grossmann & Weiss, 2021). Physical processes, including the removal
The plant-based sources that had been extensively studied to be of seed coat and size reduction, breaks down plant cells and liberates
employed as alternative proteins include legumes, such as soybean, their components. Following the removal of moisture and fat, the pro
chickpea, lentil pea, pigeon pea, pea, faba bean, cowpea, and lupin; tein is subsequently solubilized in chemical solvents in which they will
seeds, such as chia, flaxseed, and pumpkin; almonds and nuts; cereals, be completely dissolved. Amphiphilic proteins are zwitterions at iso
such as rice, millet, wheat, corn, barley, maize, and sorghum; and electric pH. Protein surfaces are negatively charged above the isoelectric
pseudocereals, such as quinoa, amaranth, and buckwheat (Sá et al., point (pI) while it is positively charged below the pI. The balance of
2020b). Oilseeds are also a good source of protein after legumes. Pre negative and positive charges at the pI reduces electrostatic forces,
dominantly consumed plant proteins like soy belong to the family of oil- causing attraction forces to aggregate and precipitate the proteins
producing crops. Some of the other proteins sourced from oilseeds and (Novák & Havlíček, 2016). This forms the basis of protein extraction at
crops include sunflower, rapeseed, canola, and safflower (Arntfield, pI. Depending on the extraction process flour, concentrates, isolate, and
2018; Arrutia et al., 2020). Some common proteins and their focus of hydrolysate protein components are obtained. Protein flours contain less
interest are depicted in Table 1. than 65% protein (Kumar et al., 2021). Isolates (>80%) often contain
Apart from the above-mentioned sources, the following plant sources more protein than concentrates (60–80%) (Embaby et al., 2018). Protein
gained significant attraction for protein extraction and modification in concentrate is derived by removing non-protein components, primarily
recent years (Tables 2 and 3). These include edible leaf proteins (Arte carbohydrates, with hydroalcoholic solutions and acidic water to
misia capillaris Thunb., ryegrass, cassava), legumes like black bean, improve protein concentration, while protein isolate is obtained by
2
N. Ravindran et al.
Table 2a
Extraction methods of Plant-based protein sources. (See below-mentioned references for further information.)
3

(continued on next page)
Table 2a (continued )
4
5
N. Ravindran et al.
6

*p: pH dependent extraction; U: Ultrasound (US); M: Microwave (MW); Z: Micellization or Moderate Electric Field (MEF); S: Separation (size reduction and electrostatic separation); E: Enzymatic; H: Pressure; M.Protein
fraction: Major Protein fraction; ANF: Anti nutritional factor
solubilizing the protein in salt water or a solution with a pH far from pI. Protein extraction using chemical methods (alkaline extraction fol
Protein hydrolysate is distinct and is composed of peptides and amino lowed by isoelectric precipitation, AE/IP) is well-known and has been in
acids formed due to protein degradation by enzymes, acids, alkaline practice for ages. The trend is mostly of the extraction (48.9%) using
treatment, or fermentation (Asaithambi, Singha, & Singh, 2022a,b, chemical methods like AE/IP and pH shift. These techniques leads to
2023; Gençdağ, Görgüç, & Yılmaz, 2020). undesired reactions, depletion of amino acids, and reduced digestibility
of proteins. Eventually, physical extraction method grew up to 35.6%
with technologies like ultrasound (bitter gourd, Dolichos lablab L.,
3.2. Methods for protein extraction
pomegranate, pumpkin seed, sesame bran, sesame meal, soybean okra,
and sunflower meal), microwave (sesame bran, sesame meal and sun
Traditional extraction methods necessitate the use of heat and a
flower meal), moderate electric field (sesame meal), pressurized liquid
solvent as a carrier. The efficiency of extraction increases with tem
extraction (pomegranate), electrolyzed water (rice bran), size reduction
perature, facilitating the transfer of chemical compounds. However,
and electrostatic separation (rapeseed meal) and micellization (hemp).
heat can lead to chemical degradation, potentially causing undesirable
Bio-extraction using enzymes (potato, rapeseed meal and rice bran)
changes. The functionality of the extracted protein is impaired owing to
accounted for 6.7% with enzymes like alcalase and protease. Combining
the protein denaturation that has occurred (Gençdağ et al., 2020). This
physical techniques with chemical methods (2.2%) and enzymatic
emphasizes the significance of maintaining rigorous control over the
treatments (6.7%), for rice bran and pomegranate (Guzmán-Lorite et al.,
process variables. Therefore, novel approaches for protein extraction
2022; Watanabe et al., 2019) and sesame bran (Görgüç, Bircan, et al.,
utilizes cutting-edge technologies such as ultrasound, microwave,
2019; Görgüç, Özer, et al., 2019; Görgüç et al., 2020) respectively,
pressurized liquid extraction, enzyme extraction, hydrotropic and deep
improved protein’s yield and its properties. When compared to other
eutectic solvent extraction, pulsed electric field, and high-voltage elec
techniques for protein extraction, ultrasound resulted in high yield of
trical discharge, and results in minimally processed products that meet
protein from pumpkin seed, sesame meal and soybean okra (Das et al.,
the customer demand. Fig. 1 represents different extraction techniques
2022; Eze et al., 2022; Mathews et al., 2023), while microwave (MW)
based on the type of extraction. There are several literatures available on
resulted in high yield of protein from sunflower meal and sesame bran
the extraction methods (Contreras et al., 2019; Kumar et al., 2021;
(Görgüç, Özer, et al., 2019; Náthia-Neves & Alonso, 2021).
Rahman & Lamsal, 2021), which falls outside the scope of this study.
The above-mentioned plant-based sources for protein were recom
mended for their applications in food as an alternative protein source for
3.3. Progression of plant protein extraction over time new product development, protein supplements, substitute for animal or
dairy proteins, emulsifiers, nutraceuticals, functional food ingredients,
Recent trends in the extraction of plant-based proteins over the infant foods, bioactive compounds (peptides with bioactivity), carriers
timeline of the past 6-7 years (2018–2024) are represented in Fig. 2. of bioactive compounds (by providing a matrix for compounds like an
From the literatures reviewed, it was evident that seeds are the pre tioxidants), biomaterials, cosmetics, and pharmaceutical industries.
dominant source for protein extraction, accounting for about 31.3%,
followed by legumes (25%), by-products (20.8%), cereals (10.4%) and
leaf proteins (6.3%) and other sources (6.3%) like tubers (potato), spices
and plantation crops (clover and coconut).
Fig. 1. Classification of protein extraction techniques.
7
Fig. 2. Current statistics of plant-based protein (2018-2024) (a) Source, pre-treatment, extraction, and modification (radially inward), (b) Literature reports on major
protein fraction and antinutritional factors.
3.4. Voids found in reported extraction studies et al., 2018; Kutzli et al., 2023; Lao et al., 2023; Subaşı et al., 2020;
Vinayashree & Vasu, 2021; Zhang et al., 2020); chlorogenic acid in
3.4.1. Protein fraction sunflower meal (Albe Slabi et al., 2020; Náthia-Neves & Alonso, 2021);
Plant proteins are primarily categorized into four, based on glucosinolates in rapeseed meal (Fetzer et al., 2018; Z. Zhang et al.,
Osborne’s solubility classification. The total plant protein comprises 2020); tannins in pumpkin seed (Vinayashree & Vasu, 2021) and cassava
albumins (water-soluble), globulins (saline-solution soluble), prolamins leaves Koch, Nielsen, Halkier, Olsen, & Møller, 1992(); saponins in
(alcohol-soluble), and glutelins (alkali-soluble). The former protein is quinoa (Van de Vondel et al., 2020); protease inhibitor in potato
responsible for physiological functions, while the rest are storage pro (Waglay et al., 2019); gossypol in cottonseed meal (Ma et al., 2018);
teins. Based on the sedimentation coefficient, plant proteins can be sinapine (Zhang et al., 2020), phenolic compounds like condensed tan
further categorized as 2S, 7S, 11S, and 15S (Arrutia et al., 2020). nins (Fetzer et al., 2018) in rapeseed meal and cyanogenic glucoside in
Knowledge on the major protein fraction is equally significant as it has a cassava leaves (Koch, Nielsen, Halkier, Olsen, & Møller, 1992)(). Uti
significant impact on the functional properties like solubility, emulsifi lizing processing techniques, such as extraction and modification, can
cation, foaming and gelation. 40% of plant proteins contain globulin as improve the digestibility and bioavailability of plant-based proteins
their major protein fraction; some plant proteins contained albumin while also reduce their antinutrient contents (Pam Ismail et al., 2020).
(7%) as well; some special cases like potato contain patatin as its major The ANFs should, as a result, be the primary focus of extraction meth
protein fraction. Literature reports major globulin fractions in soybean, odologies, which should aim to either eliminate or significantly reduce
pea, sunflower, rapeseed, hemp, panda bean, pumpkin seed, album, them to a safe level. However, based on the studies conducted, 52% of
amaranth, quinoa, sesame, soy okara and sesame bran; major albumin research on plant-based protein extraction failed to report the presence
fractions were reported in rapeseed (napins), sunflower and quinoa. of antinutritional factors in them. This lack of knowledge can negatively
Nearly 46% of studies on plant protein did not discuss or point out the impact the efficiency and effectiveness of plant protein utilization.
major protein fractions present.
Most of the plant proteins come from seeds and legumes, which are 4. Impact of pretreatments on proteins’ extraction and quality
storage bodies of plants and account for the presence of globulins
(Arrutia et al., 2020). Altering the fractionation conditions during pro 4.1. Importance of pretreatment
tein extraction will result in the modification of protein fraction. This
was evident from the studies done by Albe Slabi et al. (2020) and Subaşı Preliminary treatments to the protein sources—seeds, legumes, or
et al. (2020) on sunflower meal, where globulin was the major protein others—tend to increase the protein yield as well as its techno-functional
fraction in the former and albumin in the later. A similar case was properties. Based on scientific reports, 28.9% of protein extraction was
observed for quinoa, where globulin was the major protein fraction in carried out with pretreatments. The pretreatments reported include
the protein extracted by Mir et al., (2019a), while albumin was pre physical (dehulling, roasting, hot-pressing, cold-pressing, pre-pressing,
dominant from the results of Van de Vondel et al. (2020). Therefore, heat stabilization), chemical (solvent extraction, dephenolization,
based on the need for any functionality of any protein, the major protein phosphorus removal, pretreatment for defatting like solvent hydration),
fraction can be altered during extraction by modifying its fractionation biological (germination) and emerging techniques (subcritical fluid
conditions. extraction, radiofrequency, pulsed electric field). Table 2b enlists the
pretreatment methods carried out for protein extraction, along with
3.4.2. Antinutritional factors their respective effects.
Antinutritional factors (ANFs) refer to the biological constituents
found in plants that have the potential to impair the absorption and
4.2. Physical pretreatments
utilization of nutrients, resulting in hindered gastrointestinal function
and metabolism. Protein bodies in the cotyledon and hulls of the legume
Subjecting the plant cells to physical treatments involves the appli
seeds are where the majority of antinutritional components are pre
cation of thermo-mechanical forces such as impact, heat, pressure, and
dominantly located. The studies that have documented ANFs revealed
shear due to which the cells under high stress that results in cell
the presence of phytic acid in hemp, pumpkin seed, soybean okra,
disruption or breakage, thus promoting the extractability of protein.
sunflower and rapeseed meal, and yellow pea (Aiello et al., 2021; Fetzer
Defatting prior to protein extraction involves pressing (either hot or
8
Table 2b
Effect of pre-treatments on protein extraction and yield.
Plant source Pre-treatment Extraction Yield ANF Effect of treatment Critical/key findings References
Method %
Cassava leaf Pounding, drying pH shift 69 Tannin and cyanide Reduction of cyanide and Optimal protein extraction (Patra &
and washing of tannin content were 83.96 conditions: pH 11 at 46 ◦ C Arun Prasath,
leaves ± 0.18% and 68.51 ± for 114 min with 23.5 mL/g 2024)
1.05%, respectively, and S/L ratio
protein was 9.71 ± 0.42%
Cottonseed Hot-pressing pH shift 58.74 Gossypol (<0.012%) Degradation of large Cold-pressed (Ma et al.,
meal − RM spec. proteins; low yield with solvent extraction and 2018)
highly denatured proteins subcritical fluid extraction
Cold-pressing 65.19 High emulsifying ability, yielded high with less
Subcritical fluid 66.65 WC, and OC denatured proteins
extraction
Hemp Dehulling AE/IP 46.9 − Significantly improved Edestin − major protein (Shen et al.,
yield, structure, color, fraction (67%); dehulled 2020)
aroma and function of the HPI accumulated more
protein terpenes and less lipid
oxidation volatiles
Germination AE/IP 96.87* − Altered the composition and Purity and functional (Liu et al.,
functional behavior; properties were improved 2023)
significant degradation of with 3 days of germination;
seed storage proteins self-stable gels are formed
Pea (yellow) Roasting AE/IP 11.5 Phytic acid Altered tertiary structure, Controlled roasting at (Lao et al.,
improved the solubility and 150◦ C for 10 or 20 mins 2023)
emulsion ability of the gave yield with high purity;
isolate long roasting time
compromised extraction
efficiency
Perilla Cold-pressing pH shift 67.87 − Low particle size, highest Nanoparticles from cold- (Zhao et al.,
foamability, solubility pressing isolated protein 2021)
emulsification, and water had excellent capacity to
holding capacity stabilize Pickering
Hot-pressing 73.48 Highest oil holding capacity emulsions
Solvent extraction 70.65 Highest creaming index
Rapeseed Cold-pressing Salting in 52.3 Phytic acid, High ratio of denatured Multi-stage enzymatic (1% (Fetzer et al.,
Enzymatic 59.5 glucosinolates and protein in pretreated meal Protease A-01) extraction 2018)
Enzymatic 80.7 phenolic compounds enables the enzyme to at a strong pH (11–12)
Pre-pressing Salting in 36.7 liberate proteins from yielded high protein
Enzymatic 60.6 insoluble protein aggregates
Enzymatic 78.3 (PP > CP)
Hydroalcoholic oil − − − Increased the meal protein Isopropanol removed most (Morgane
extraction content by 13% glucosinolates from the et al., 2019)
meal than ethanol
Cold-pressing pH shift 65.08 Phytic acid, − Extraction pH 9.0 and (Z. Zhang
glucosinolatesand precipitation pH 4.5 led to et al., 2020)
sinapine high extractability;
Globulin – major protein
fraction
Rice bran Heat stabilization Combined 65.1 − Improved yield and purity; pI of pH 3.5 at 50◦ C with (Watanabe
and Phosphorus isoelectronic decreased insoluble 0.5% alkali concentration et al., 2019)
removal precipitation and phosphorus compounds in recovered quality protein
electrolyzed water the protein concentrate with excellent amino acid
treatment score
Radiofrequency Enzyme assisted 58.8 − Reduced the yield, purity, Only higher structure levels (Ling et al.,
extraction solubility and foaming were altered; decreased 2019)
ability due to high denaturation temperature
temperature (>100◦ C); and protein enthalpy
improved absorption and
emulsification
Ryegrass Pulsed electric pH shift 31 − Enhances the release of Crude protein content (Guo et al.,
(Lolium field proteins, carbohydrates, increased to 37.3 g/100 g 2022)
perenne) and lipids, saccharides, and in dry matter; precipitated
white clover minerals from plant cells, sediment contained vital
blend with increased juice yield minerals like Ca, K, Na, Mg
by 25% and P
Sesame meal Pretreatment for − − − Solvent hydration and Use of IPA as the extraction (Capellini
defatting extraction temperature solvent (50–80◦ C), resulted et al., 2019)
impacts protein solubility. in protein-rich meal with
well-preserved functional
properties
Sunflower meal Dephenolization Ultrasound 87 Phytic acid (ND) A shift in isoelectric point US extraction of (Subaşı et al.,
from 4.37 to 4.82, affecting dephenolized meal 2020)
the protein purity and improved foaming
ζ-potential capacity, structural
stability and lowered
hydrophilicity
*AE/IP: Alkaline Extraction followed by Isoelectric Precipitation
9
cold) crushed seeds to extract oil or fat. The high temperature during hot purity and solubility. Although, the emulsification and fluid absorption
pressing denatures the proteins and results in proteins with high oil abilities were enhanced (Ling et al., 2019). H
absorption capacity (OAC) but less yield and poor quality. Hence, most Based on the reviewed literatures, it can be suggested that cold
of the work focuses on cold pressing where protein yield was high, and pressing enhances protein yield and quality. The potential integration of
denaturation was less. The pretreatment also improved the functional cold pressing with other emerging technologies and the subsequent ef
properties of proteins from cottonseed, perilla and rapeseed (Fetzer fects requires further investigation in future research.
et al., 2018; Ma et al., 2018; Zhang et al., 2020; Zhao et al., 2021).
Pretreatments like dehulling and roasting of seeds of hemp and pea 5. Trends and techniques in plant protein modification
modified their protein structure as a result of impact and heat respec
tively; simultaneous improving in yield, color, functionality and aro Any process that has the potential to induce structural reconfigura
matic profile (Lao et al., 2023; Shen et al., 2020). Considering the tion in proteins has an effect on the hydrophobic/hydrophilic equilib
negative-effects of heat observed from the results of blanching, soaking rium on the protein’s surface. This can influence the protein’s solubility
in boiling water and drying, mechanical treatments like pounding, as well as its water/ oil absorption capacities. Protein modification is an
moderate temperature drying (40◦ C for 5 h) and washing with cold approach used to alter the molecular structure or chemical composition
water were found promising for detoxification (removal of cyanide of proteins by applying specific techniques to increase their function
toxin) of cassava leaves prior to protein extraction (Patra & Arun Pra ality and bioactivity (Langyan et al., 2021). Modifications of plant-based
sath, 2024). proteins enable them to serve as a multi-functional versatile ingredient
and develop a wide range of functional food systems. It also helps to
4.3. Chemical pretreatments address the existing limitations by altering their physicochemical and
functional properties.
Subjecting the plant cells to chemical treatment before extraction
helps in disrupting the cellular structure, providing access to the cell
5.1. Current trends in plant protein modification
components, and promoting the extraction yield. The chemicals or sol
vents used for treating the plant tissue sometimes remove the soluble
The present study evaluated the distribution of protein modifications
compounds in it, for example, hexane solubilizes the fat compounds.
(Fig. 2) as follows: physical modifications comprised a total of 40.6%,
Chemical pretreatments generally include defatting, alcoholic treat
chemical modifications for 8.7%, enzymatic modifications for 10.1%,
ments and specific treatments for removal of undesirable compounds
novel modifications such as complexation and fibrillization for 11.6%,
(such as polyphenols) that facilitates in protein extraction. Studies show
physicochemical modifications for 21.7%, physical-enzymatic modifi
that pretreatments done to defatted meals like hydroalcoholic treat
cations for 2.9%, physical modifications combined with novel tech
ments (a mixture of isopropanol or ethanol with water) and prewash
niques for 1.4%, and chemical modifications combined with novel
using water with pH near the isoelectric point before protein extraction
techniques for 2.9%. Cold plasma is classified under innovative
reduced the anti-nutritional factors while improving protein solubility
methods, however, due to the mechanism of action in protein modifi
(Fetzer et al., 2020; Morgane et al., 2019). Few studies also reported
cation, in Fig. 2, it is grouped under physical modification techniques.
changes in the yield of protein from defatted seed meal due to the pre
Pea (Chao et al., 2018; Chen & Campanella, 2022; Klost & Drusch,
treatments done before oil extraction, the change of solvents used for oil
2019; Sha et al., 2021; Shah et al., 2019; Zha et al., 2019; Zhang et al.,
extraction, and the removal of phosphorous and phenolic compounds
2022; S. Zhang et al., 2021), soy (Huang et al., 2019; Tan et al., 2021;
from the meal. Apart from the yield, these treatments enhanced the
Yan et al., 2021; Zhang et al., 2020; Zhou et al., 2020), sunflower seed
solubility and purity of protein, as the undesirable components are
(Dabbour et al., 2021; Malik & Saini, 2018, 2019; Subaşı et al., 2020;
removed (Ma et al., 2018; Morgane et al., 2019; Subaşı et al., 2020;
Subaşı et al., 2021), hemp varieties (Karabulut & Yemiş, 2022; Kutzli
Watanabe et al., 2019).
et al., 2023; Rawat & Saini, 2023), and rice (Ding et al., 2022; Jia et al.,
2022; Nisov et al., 2020; Zhang et al., 2018) have been identified as the
4.4. Biological pretreatments
primary protein sources selected for modification in light of their
abundance, substantial production output, and desirable protein qual
Soaking before protein extraction causes hydration of the plant cells
ity. Several studies have reported on the modifications with a focus on
thereby aiding the loosening of seed coat or hul. It helps in leaching out
enhancing the solubility, emulsification, and gelling properties of
the water soluble antinutrients such as tannins and saponins. Germi
proteins.
nating the seeds followed by soaking also reduces the antinutritional
factors, thereby altering the protein composition and improving the
yield and purity of protein. Soaking and germination made a notable 5.2. Techniques for modifications
reduction of anti-nutritional components such as tannin and phytic acid
and enhanced the nutritional and bioactive potential of the pseudocer Protein modification techniques can be categorized as physical,
eals amaranth, buckwheat and quinoa (Thakur et al., 2021). Gelation of chemical, biological, or other novel techniques (Fig. 3) and the effects of
hemp proteins was also improved with germination (Liu et al., 2023). these modifications on plant proteins are illustrated in Table 3.
When pressed meals are subjected to enzymatic extraction, high yield
was observed which may be due to cell structure damage during pressing 5.2.1. Physical modifications
and/or the ability of enzyme to release protein from the damaged cell Physical modification refers to alterations primarily in the structure
(Fetzer et al., 2018). of a substance, resulting in the loss of structural integrity due to dena
turation in case of proteins. Since no chemicals, enzymes, or microbes
4.5. Emerging technologies are involved, these protein modification techniques are deemed safe and
have garnered considerable attention, thereby circumventing any po
Treating the plant source with emerging technologies such as tential repercussions associated with the presence of chemical residues.
subcritical fluid extraction improved the yield and functional attributes
of protein (Ma et al., 2018). Pulsed electric field accelerated the release 5.2.1.1. Thermal modification. Heat-induced modifications (conven
of proteins from the cells leading to high yield. This kind of pre tional heat, microwave, infrared, radio frequency, and ohmic heating)
treatments can be employed to extract juices as well (Guo et al., 2022). cause alterations primarily in the structure by denaturation and
However, radiofrequency (RF) had an adverse effect on protein yield, unfolding of amino acid chains by weakening and splitting hydrogen
10
Fig. 3. Plant protein modifications: A) Physical B) Chemical C) Biological and other novel approaches.
and disulfide bonds, forming protein aggregates. Thermal modifications strength tends to reduce the protein solubility due to excessive oxidation
by applying heat to album (Mir et al., 2020), manila tamarind (Singh & by free radicals produced by electrochemical processes and protein ag
Sit, 2023), and quinoa (Van de Vondel et al., 2021) proteins reduced gregation. This also aggravates other functional properties (Taha et al.,
their solubility due to protein denaturation and aggregation and altered 2022). Combination of PEF with alkaline pH shift enables modification
their surface hydrophobicity. Ma et al. (2022) utilized heat-assisted pH in highly solubilized state. The resulting functionality was much better
shift to improve the emulsification properties of coconut proteins. due to limited protein oxidation and subsequent protein unfolding by
Thermal stability and gelling behavior of plant proteins (pea, sunflower polarization, and opens up a novel avenue in dual modification tech
and album) were also significantly enhanced by heat (Chen & Campa nique (Wang et al., 2023).
nella, 2022; Malik & Saini, 2019; Mir et al., 2020), except for autoclave MEF (electric field strength < 1000 V/cm) effects can be categorized
and microwave heat that resulted in poor gelling properties due to their into two: with generation of heat (ohmic heating) and without genera
poor solubility and syneresis (Mathews et al., 2023; Singh & Sit, 2023). tion of heat/ non-thermal effect (n-MEF). Literature reveals that ohmic
Applying moist heat through autoclave denatures and alters the heating possesses the ability to alter the protein’s denaturation and
secondary and tertiary structures of protein by weakening hydrogen aggregation pathways, gelation behavior and interacting mechanisms.
bonds and functional groups, thereby disrupting the structural integrity This opens novel avenues for the development of diverse protein systems
and reducing its functionality (Singh & Sit, 2023); whereas application such as gels, films, and nano/microstructures with desirable function
of moist heat through extrusion improves the functional properties and ality. Most of the plant protein modifications done using ohmic heating
induce shape and texture modifications (Pavani, Singha, Rajamanickam, are associated with soy and its related products, and significant changes
& Singh, 2023). High moisture extrusion (>50% moisture content) and were observed in their techno-functional properties (Avelar et al.,
shear cell technology are predominantly employed in the development 2021). However, ohmic heating modifications on other plant proteins
of plant-based meat analogues as the proteins undergoes still remain an unexplored area. Contrarily, n-MEF based modifications
thermo-mechanical stresses (high temperature and high shear) and are booming in plant proteins. n-MEF assisted modification of sunflower
hence results in fibrous end products (Cornet et al., 2021). Physical (Subaşı et al., 2021) and sesame (Mathews et al., 2023) proteins reduced
modifications that involve heat such as microwave, radio frequency and their particle size, denaturation temperature and enthalpy. With n-MEF,
infrared helps in enhancement of protein unfolding, digestibility and the proteins are less denatured, and their interfacial surface tension is
functionality (Langyan et al., 2021). significantly brought down, leading to high emulsification ability.
5.2.1.2. Electric-field based modification. Electric field-based techniques 5.2.1.3. Ultrasound modification. Ultrasound (US) is a green and sus
encompass pulsed electric field (PEF) and moderate electric field (MEF). tainable technique that significantly enhances protein yield, solubility,
The mechanism to modify protein by both the techniques remains same: and techno-functionality. The cavitation created during ultrasonication
1. electroporation and 2. internal heating. When a cell membrane is disrupts only the non-covalent bonds inducing alterations in the struc
subjected to electric field, pores are formed when the field strength ture and reducing particle size. It destroys the secondary, tertiary, and
exceeds the strength of cell membrane; it hampers the intact cell wall quaternary structure levels, leaving the primary structure unaltered
and results in protein denaturation which leads to unfolding and alter (Barbhuiya, Singha, Asaithambi, & Singh, 2022; Barbhuiya, Singha, &
ations in the secondary and tertiary structure. Unfolded proteins involve Singh, 2021). The radicals and superoxide produced during cavitation
in subsequent interactions and aggregate, limiting their solubility cause cross-linking in proteins. An increase in sulfhydryl (− SH) groups
(Mathews et al., 2023). can be attributed to their partial unfolding and subsequent exposure of
PEF (electric field strength 20–100 kV/cm) causes vibration of polar their concealed –SH groups to the surface and the reduction of disulfide
groups in the protein chain, weakening the hydrogen bonds, resulting in (S–S) bonds to –SH groups caused by cavitation (Rawat & Saini, 2023).
reduction of β-turns and increase in antiparallel β-sheets. Application of As a result, among majority of the studies examined, about 61%, relied
PEF to plant proteins like soy, canola, pea and sunflower modified their on US for protein modification, either as an individual method (high
structural and functional properties. The change in the protein proper intensity ultrasound, HIUS or dual frequency ultrasound or fixed/
ties depends on the electric field strength. Most of the studies showed random-sweeping frequency ultrasound or simply ultrasound) or in
promising results for moderate PEF (10 kV/cm) as increased field conjunction with other techniques.
11
Table 3
Plant protein modifications.
Protein Treatment Functional Modifications Other Key Findings References
EA S WHC OHC FA G PS ZP SH
Amaranth Alkaline pH shift þ þ ¡ þ þ Alkaline pH shift with US caused notable (Figueroa-

Acid pH shift ¡ ¡ þ þ þ structural modification and improved González et al.,
US þ þ ¡ ¡ þ protein digestibility due to protein 2022)
Al.pH shift + US þþ þþ ¡ þ þ disaggregation
Ac.pH shift + US ¡ ¡ þ þ þ
Album High–intensity þ þ ¡ þ US (20 kHz, 500 W and 25% amplitude) (Mir et al.,
ultrasound (HIUS) increased loss of molecular weight and 2019b)
whiteness index; reduced enthalpy and
denaturation temperature
Heat þ þ þ Controlled heat treatment (100◦ C for 30 (Mir et al., 2020)
min) led to structural changes that
improved thermal stability, color and in
vitro digestibility
Black bean Enzymatic (2 %) All hydrolysates possessed antioxidant (Zheng et al.,
Alcalase þ þ potential; alcalase and bromelain formed 2019)
Bromelain þþ þ higher degree hydrolysate
Ficin þ þ
Camelina and US þ þ þ þ þ ¡ þ US frequency of 40 kHz for 20 min (Ngo & Shahidi,
Flixweed improved functional properties, 2021)
comparable to soy
Chickpea, Lentil Enzymatic( ¡ Alcalase showed high degree of (Xu et al., 2021)
pea, Pigeon alcalase) hydrolysis; both enzymes enhanced
pea Enzymatic(b þ þ ¡ antioxidant and anti-inflammatory
romelain) properties of legume proteins
Chickpea US-assisted pH shift ¡ þ þþ ¡ ¡ þ US (300 W, 20 kHz for 5 mins at 30◦ C) of (Wang et al.,
pH (12) shifted protein significantly 2022)
altered the structure and reduced
interfacial tension, forming more stable
interfaces
Coconut Heat + pH shift þþ ¡ þ þ Solubility decreased with increasing heat (Ma et al., 2022)
and pH near pI; best emulsifying stability
− pH 11 with 90◦ C due to aggregates
formed by cross-linking of covalent bonds
Coconut milk US-assisted pH shift þ ¡ þ þ US (40 W/L and 53 kHz for 20 min) with (Sun et al., 2022)
pH 12 increased the viscosity and thermal
stability of milk
Faba bean US-assisted pH shift þþ þ þ þ þ ¡ þ + US (1200 W, 20 kHz for 20 mins) at pH 11 (Alavi et al.,
disrupted larger aggregates into smaller 2021)
ones and significantly altered the
structure; formed strong viscoelastic
interfacial film with high stability
Flaxseed High hydrostatic þ HHP at 300 MPa for (Franck et al.,
pressure-assisted 10 min with trypsin enhanced degree of 2019)
enzymatic hydrolysis and bioactive peptide yield
(antioxidant)
Atmospheric pressure þ þ Limited exposure time (5 kV for 5 to 10 s) (X. Yu et al.,
plasma jet yielded high in vitro antioxidants and 2020)
released phenols and flavonols
Garden cress Enzymatic þ þ þ Significant improvement in antioxidant (Mulla & Ahmed,
seed meal (alcalase) levels with moderate hydrolysis (10.69%) 2019)
Ginkgo pH shift þ þ ¡ þ þ High solubility was observed at pH 11; (W. Zhang et al.,
high emulsification at pH 2 due to protein 2021)
adsorption at the oil–water interface
Grass pea DBD-cold plasma þþ þ ¡ ¡ þ CP (18.6 kVpp for 60 s) caused high (Mahdavian
(Lathyrus etching and formed more orderly Mehr &
sativus L.) secondary structures, improved thermal Koocheki, 2020)
and emulsion stability
Hemp High–intensity þ þ ↔ þ þ ¡ ¡ þ HIUS intensity of 37 W/cm2 for 7.8 min (Karabulut &
ultrasound was optimal; altered tertiary structure was Yemiş, 2022)
observed
Amyloid fibrillization þ Heating (90◦ C) at pH 2 with stirring (300 (Kutzli et al.,
rpm) for 4 h formed relatively flexible 2023)
amyloid fibrils
Manila Ultrasound þ þ þ þ ¡ þ US (180 W and 35 kHz) increased particle (Singh & Sit,
Tamarind density 2023)
Autoclave (AC) ¡ ¡ ¡ ¡ ¡ AC (121℃ and 15 psi) reduced particle
density and altered the hydrophobicity/
hydrophilicity balance
US + AC / AC + US þ þ þ þ ¡ þ Increased darkness and bulk density
Pea High hydrostatic þ ↔ þ ¡ HHP (600 MPa) led to significant changes (Chao et al.,
pressure in protein structure and increased protein 2018)
aggregation
12
Table 3 (continued )
Protein- þþ þ ¡ þ ¡ Controlled Maillard reaction (glycated (Zha et al., 2019)

polysaccharide with gum Arabic (1:4) for 1 day)
conjugation improved emulsion stability due to steric
hindrance effects of the conjugates;
prevented emulsion oxidation and volatile
compound formation
Acylation þþ þ þ ↔ þ þ þ Acylation with succinic anhydride (Shah et al.,
enabled it to act as an emulsifier (egg 2019)
replacer) in cakes
Enzymatic (trypsin) þ þ ¡ þ Hydrolysis enhances interfacial film (Klost & Drusch,
strength and in-plane structural 2019)
rearrangements
Atmospheric cold þ þþ þ þ Plasma treatment used relatively low (S. Zhang et al.,
plasma temperature (80–90◦ C) for denaturation 2021)
for 30 min and formed stable gels
High–intensity þþ þ ¡ þ þ US (50% amplitude and 57–60 W/cm2 for (Sha et al., 2021)
ultrasound 5 min) resulted in less elastic interfacial
film but with enhanced emulsion stability
Enzymatic (Alcalase) þ þþ ¡ Alcalase 2.4 L (~30 μL) treatment at pH 7 (Chen &
for 3 min formed hydrolysates; fine, Campanella,
porous, and firmer gels were formed at 5% 2022)
protein content under mild heat (85◦ C, 10
min)
HIUS-assisted pH þþ þþ ¡ þ þ US (500 W, 20 kHz, 10 min) at pH 12 (Zhang et al.,
shift enhanced the adsorption of protein at the 2022)
oil/water interface; interfacial film was
strong and compact; emulsion was less
prone to phase separation due to the
intermolecular forces that resisted droplet
coalescence
Peanut pH shift þ þ þþ ¡ þ þ Significant improvement in breaking (J. Li et al., 2020)
force and WC of the gel formed by pH 10
shifted isolate
Peanut (high Cold plasma assisted þ ¡ Glycation via Maillard reaction with less (J.-j. Yu et al.,
temperature glycation degree of browning; thermally stable and 2020)
press flour) more ordered conjugate was formed
Perilla Dynamic high- þ þ þ þ þ ¡ ¡ þ DHPM at 120 MPa showed superior (Q. Zhao et al.,
pressure techno-functional attributes; structural 2021)
microfluidization rearrangement due to microfluidization
exposed the hydrophobic groups
US-assisted pH shift þ þþ þ ¡ ¡ þ US (20 kHz at pH 12) enhanced the (Yang et al.,
adsorption rate and elastic modulus at the 2022)
oil-/ air–water interfaces, due to modified
secondary structure
Potato High-intensity þ þ þ ¡ þ þ US (600 W, 20 min) increased digestibility (Hussain et al.,
ultrasound and antioxidant activity; decreased foam 2021)
stability
Pumpkin High-intensity þ þ ¡ þ US caused highly disordered structure; an (Du et al., 2022)
ultrasound increase in US power, increased
brightness and decreased turbidity
Quinoa Hydrothermal ¡ þ Non-covalent protein aggregation at (Van de Vondel
70◦ C, pH 5.0; covalent protein et al., 2021)
aggregation at 100◦ C, pH 7.0; loss of
solubility due to protein aggregation
Rapeseed Protein- þ þþ þ Glycated with dextran; high thermal (Wang et al.,
polysaccharide stability 2018)
conjugation
Acylation þ þþ þ Acylated with butanedioic anhydride;
high ordered structure and thermal
stability; low degree of acylation
improved gelation compared to glycation
Rice US assisted alkali þ þþ þ ¡ ¡ − Solubility increased to a maximum value (Zhang et al.,
treatment of 19.79 mg/mL at an alkali concentration 2018)
of 0.08 M
US + enzyme ¡ þ Fixed and random-sweeping frequency US (Ding et al.,
(120 W/L and 27.3 kHz) in presence of 2022)
alcalase (3780 U/g) enhanced degree of
hydrolysis and ACE inhibitory activity
High hydrostatic þ þ ¡ Soluble aggregates formed by covalent (Jia et al., 2022)
pressure assisted bonding between rice glutelin and D-
glycation xylose; moderate pressure improved
emulsification and antioxidant activity
Acetylation þ þ þ ↔ ¡ Acetylation with 40% acetic anhydride (Miedzianka
increased the protein content with et al., 2023)
modified protein fractions
13
Table 3 (continued )
Rice endosperm Enzymatic þ þ þ þ þ ¡ ¡ ¡ Neutral (pH 7) and acid endoprotease (pH (Nisov et al.,
(endoprotease) 5) (20 U) treatment for 3 h hydrolysed 2020)
protein upto 55.2% and 42.7%
respectively; high colloidal stability was
observed for the former.
Sesame meal Ultrasound þ þ þ þ þ þ ¡ þ In vitro protein digestibility raised due to (Mathews et al.,
Microwave þ ¡ þ þ þ ¡ ¡ þ protein structural denaturation enhancing 2023)
Moderate electric þ þ þ þ þ þ ¡ þ the enzyme accessibility and is higher for
field MW (94.44%), followed by US (93.25%)
and MEF (91.64%); poor gelling of MW
due to poor solubility
Soy US + acid þþ þ þ þ US (200 W and 20 kHz) at 0.001 M HCl for (Huang et al.,
10 min improved emulsion stability; PS 2019)
increased due to aggregation
pH-shift + Protein- þ þ þ pH 12 alters the protein structure and (Yan et al.,
polyphenol increases the sulfhydryl group; this 2021); (Zhou
conjugation enhances protein/polyphenol binding via et al., 2020)
(Polyphenol: non-covalent interactions, protecting the
epigallocatechin-3- antioxidant ability of EGCG and
gallate or EGCG) improving its bioavailability; covalent
complexes possessed higher thermal
stability, anti-digestive ability, oxidation
resistance and polyphenol-protection
Atmospheric cold þ þ þ þ þ þ Plasma exposure (120 Hz for 5 min) (Q. Zhang et al.,
plasma reduced the IgE-binding level of up to 2020)
75%
Amyloid fibrillization þþ þ Increase in particle size occurred due to (Wang et al.,
prolonged incubation of 3 days 2020)
High hydrostatic þþ þþ ¡ þ þ High pressure (400 MPa) under extreme (Tan et al., 2021)
pressure + pH-shift pH (11) forms small emulsion droplets
with high stability
DBD-cold plasma þ þ þ þ Treatment of 18 kV for 15 min was found (Sharafodin &
optimal, but thermal effect was observed; Soltanizadeh,
effect of mechanical forces of corona wind 2022)
influenced the structure
Pulsed electric field þ þ þ ¡ þ þ pH 11 with moderate PEF strength (10 (Wang et al.,
+ pH shift kV/cm) caused unfolding of proteins and 2023)
aggregate formation
Atmospheric cold þ þ Alters secondary and tertiary structure; (Dabade et al.,
plasma (pin-to-plate) significant reduction of trypsin inhibitor 2023)
activity, leading to improvement in
digestibility
Amyloid fibrillization þ þ Ordered β-folded structures increased to (Yu et al., 2024)
53.61% with increase in heating time for
24 h
Sunflower High–intensity þ þþ ¡ þ Probe US showed higher effect on the (Malik & Saini,
ultrasound rheological and structural changes, 2018)
increased thermal degradation and
reduced crystallinity
Heat + pH shift þ þ þ Gel strength improved with heating when (Malik & Saini,
(around pI 4.5) moved away from pI (pH 3.5 and 5.5); 2019)
heat caused structural changes, improved
thermal stability and reduced crystallinity
Sunflower meal Moderate electric ¡ + Surface tension was reduced by 10% for (Subaşı et al.,
field 0.2% w/w SPI by applying 150 V for 20 s; 2021)
denaturation temperature and enthalpy
also decreased
Ultrasound þ ¡ þ þ Improved structural and foam stability (Subaşı et al.,
and lowered hydrophilicity were 2020)
observed
Dual frequency þ ¡ þ ¡ þ þ Dual frequency US (20/28 kHz) at 50◦ C (Dabbour et al.,
ultrasound was more efficient than mono frequency 2021)
US due to enhanced mass transfer and
extractability
Sunn hemp High–intensity þ þ þ þ þ ¡ þ þ US at 50% amplitude for 20 min was used; (Rawat & Saini,
ultrasound negative zeta potential due to high no. of 2023)
negatively charged amino acid groups
Turtle bean pH-shift þ ¡ ¡ þ þ þ þ Low pH (1–3) caused structural changes (He et al., 2020)
(black) that led to improved digestibility and
reduced immunoreactivity
Wheat germ Atmospheric cold þ þ þ ¡ þ Plasma treatment at 25 kV for 5 min in (Abarghoei et al.,
plasma basic pH was suggested for better 2023)
functionality
*EA: Emulsifying ability; S: Protein solubility; WHC: Water holding capacity; OHC: Oil holding capacity; FA: Foaming ability; G: Gelation; PS: Particle size; ZP: Zeta
potential; SH: Surface hydrophobicity.
**++ denotes special focus on improving the specific property; + denotes increase; − denotes reduction; ↔ denotes no change.
14
Based on the observations from the reviewed literatures (Table 3), 5.2.2. Chemical modification
the key finding is that the US treatment reduces the particle size and Proteins can undergo chemical modifications by introducing new
enhances the solubility, oil and water absorption capacities, foaming functional groups or removing existing components from their structure.
ability, and surface hydrophobicity of proteins; few studies (Dabbour The chemical modification techniques can be grouped into non-additive
et al., 2021; Karabulut & Yemiş, 2022) also reported a drop in water (deamidation) and additive (glycation, phosphorylation, acylation,
holding capacity. Emulsifying ability is positively correlated with cationization, and pH shifting) treatments. Most chemical modification
interfacial surface tension and is improved in various plant species, techniques raise concerns regarding regulation and clean labeling due to
including camelina and flixweed, faba bean, hemp, manila tamarind, their utilization of chemicals and subsequent production of chemical by-
pea, perilla, potato, rice, sesame, and Sunn hemp, by application of ul products in most instances. Hence, specific methodologies exhibit
trasound; conversely, there is an inverse trend in chickpea and the limited suitability for food-related purposes.
water-soluble fraction of pea protein isolate, where emulsification was
diminished. Often, ultrasound is used to enhance emulsification, and 5.2.2.1. Additive chemical modification. Glycation: Maillard reactions
only a small number of studies have linked US modification to the gel or enzymatic cross-linking cause glycation, or glycosylation respec
ling property of proteins. Gelation of sesame and sunflower proteins was tively, where the carbonyl group of a reducing sugar covalently binds to
strengthened by US (Malik & Saini, 2018; Mathews et al., 2023) whereas the free amine group of the protein through controlled heating in the
it was reduced for hemp protein (Karabulut & Yemiş, 2022). presence of water; the process results in molecular structural changes
The combined application of ultrasound is frequently employed in that immunomodulate plant-based proteins. Ultrasonication, high hy
conjunction with pH modulation and enzymatic action. The former drostatic pressure, microwave, irradiation, electrospinning, cold
combination demonstrates notable efficacy in enhancing protein solu plasma, and spray drying are novel methods for glycating plant-based
bility. Especially, when subjected to an alkaline pH shift, increased proteins. Glycation can lead to the development of a denser adsorbed
solubility and improved foaming ability were reported when compared interfacial layer, which can offer steric and/or electrostatic hindrance.
to ultrasound alone. The solubility of rice, pea, and perilla proteins was This can be associated with the improved emulsifying ability of proteins
found to be improved through the application of ultrasound-assisted pH derived from plants. Studies on glycation of rapeseed proteins with
shift techniques, as demonstrated by Zhang et al. (2018), Zhang et al. dextran produced modified proteins with enhanced gelation and ther
(2022) and Yang et al. (2022), respectively. Regarding emulsification, mal stability (Wang et al., 2018). According to Zha et al. (2019), the
Huang et al. (2019), Alavi et al. (2021), and Zhang et al. (2022) controlled Maillard reaction used to glycate pea proteins with gum
employed ultrasound-assisted pH shift to modify the emulsifying ability Arabic produced a heterogeneous microstructure, reduced the amount
of faba bean, pea, and soy proteins. Conversely, when subjected to an of free amino acids, and increased relative solubility and emulsifying
acidic pH shift, the treatment exhibited a reduction in solubility and ability. Hydrothermal cooking with D-xylose, followed by HHP treat
foaming ability (Figueroa-González et al., 2022; Huang et al., 2019). ment, glycates rice proteins, enhancing their emulsifying behavior; the
This is due to the formation of aggregates at low pH, potentially around resulting products showed a low browning intensity and a high grafting
the protein’s isoelectric point, which increased the protein size because degree (Jia et al., 2022).
of the US-assisted acidic pH shift. The later conjunction is associated Phosphorylation: The addition of phosphate groups to a protein’s
with improved hydrolysis and bioactivity (Ding et al., 2022). primary sequence has a powerful effect on its function. The protein’s
conformation and structure change, when the phosphate group cova
5.2.1.4. High pressure processing. Application of high pressure to pro lently bonds to an amino acid residue, affecting its functionality and
teins breaks the existing hydrophobic and electrostatic interactions and stability. The added phosphate group increases the electronegativity and
forms new bonds, which lead to aggregation and gelation. As a result of electrostatic repulsion between protein molecules, improving their
denaturation, the –SH groups are exposed, attributing to an increase in functional properties. Additionally, it preserves the nutritional
hydrophobicity and low solubility. HPP solely affects the non-covalent bioavailability. The most commonly used phosphorylation reagent is
bonds, such as ionic, hydrogen, and hydrophobic bonds, while the co sodium tri metaphosphate (STMP), which is GRAS-safe. STMP phos
valent bonds, which possess restricted flexibility under high pressure, phorylation improved the functionality of rice glutelin, potato, soy,
remains unaffected. This leaves the primary structure of protein intact. peanut, and pea protein (Nikbakht Nasrabadi et al., 2021). Very limited
According to the findings reported in scientific literatures, the modifi research was found in this technique during the reviewed timespan.
cation of the primary structure of proteins requires an extremely high Acylation: Proteins are acylated using acyl anhydrides and halides.
pressure exceeding 2 GPa, whereas the secondary and tertiary structures The acylating agent—acetic or succinic anhydride—classifies the pro
of proteins can be altered at relatively lower pressures, specifically cess as acetylation or succinylation. Acylation increases the molecular
above 400 MPa and 100–200 MPa, respectively (Avelar et al., 2021). weight, gelation, and surface charge of plant-based proteins, making
Modifications employing high pressure include techniques like high them more hydrophobic and functional without reducing their nutri
hydrostatic pressure, HHP and dynamic high-pressure fluidization, tional value. Butanedioic anhydride acylation of rapeseed proteins
DHPF. It can be suggested (from Table 3) that dynamic high-pressure produced carboxyl-propionylated reactions, highly ordered structure,
microfluidization is efficient than high hydrostatic pressure treatment and slight changes in free sulfhydryl content and surface hydrophobic
as it improves all the functional properties; microfluidization exposes ity; limited acylation improved gelling (Wang et al., 2018). Pea protein
the hydrophobic groups due to structural rearrangement (Chao et al., (PP) succinylation with n-octenyl, dodecenyl, and succinic anhydride
2018; Franck et al., 2019; Jia et al., 2022; Tan et al., 2021; Zhao et al., (SA) improved protein functionality, and the PP-SA derivative was a
2021). HHP (300–400 MPa) treatment to pea, soy and rice improves its good emulsifier, which replaced eggs and soy lecithin in cake produc
solubility, emulsification, and emulsion stability (Chao et al., 2018; Jia tion, improving quality and acceptability (Shah et al., 2019). Similar
et al., 2022; Tan et al., 2021). Overall, high pressure decreases particle results were obtained on acetylating rice proteins with acetic anhydride
size, modifies texture and solubility, and improves the fluid binding which improved their emulsifying properties, solubility and water
capacities, colloidal stability, and antioxidant activity. holding capacity (Miedzianka et al., 2023).
Overall, all the modifications mentioned above improve the func Cationization: The addition of quaternary ammonium groups to
tionality of proteins by enhancing their thermal stability, surface hy proteins causes cationization. As a result of the incorporation of cationic
drophobicity, gelling, foaming, emulsifying ability, nutritional value, moieties onto the surface of the protein, its technological functionality
and digestibility. Eliminating antinutritional factors reduces immuno was altered, including its solubility and emulsification capabilities.
reactivity and allergenicity. Additionally, the encapsulating capabilities of soy protein and sunflower
15
protein were improved (Nikbakht Nasrabadi et al., 2021). This method Nasrabadi et al., 2021). Some of the enzymes and their modification
of modification is rarely taken into consideration and investigated. sites are mentioned in Table 4.
pH shifting: As discussed earlier, the pH level of the aqueous me Based on the literatures reviewed, enzymatic hydrolysis is a more
dium in which proteins are solvated plays a pivotal role in determining prevalent technique for protein modification compared to enzymatic
their conformation. Modifying the acidity or alkalinity (achieved by crosslinking. Enzymatic hydrolysis of plant proteins was extensively
chemical additives like HCl and NaOH) of the environment can induce done for legumes like pea, chickpea, lentil pea, pigeon pea, black bean,
alterations in the structural and functional properties of proteins. Pro other sources like rice, rice endosperm, flaxseed and garden cress seed.
teins unfold and expose sulfhydryl and hydrophobic regions at extreme The enzymes used for this purpose were alcalase, bromelain, ficin,
basic pH values, allowing novel protein interactions. Acidic treatment proteases (both endo and exo), and trypsin. Interestingly, alcalase
exposes protein to low pH values, which might cause it to unfold and emerged as the enzyme of choice due to its potential to cleave amide
refold after pH normalization. This kind of behavior was observed in bonds and facilitating the interaction of amino groups to form aggre
amaranth, soy and sunflower (Figueroa-González et al., 2022; Huang gates. It also showed higher degree of hydrolysis when compared to
et al., 2019; Malik & Saini, 2019). Thus, most research used basic pH
because proteins are soluble at higher pH values. Black turtle bean,
Table 4
ginkgo, and amaranth proteins were modified using pH shift (Figueroa-
Enzymes and related protein modifications.
González et al., 2022; He et al., 2020; Zhang et al., 2021). Li et al. (2020)
Enzymes Cleavage sites Modification Applications
utilized pH shift to enhance the gelation behavior of peanut protein.
Since pH-shifting treatments induce protein reactivity by fostering its Trypsin Only near the Surface-active Pea and oat
unfolding, they can also be used as a pretreatment for other modification positively charged properties; protein
amino acids lysine improvement of
techniques. Recent studies employed pH shift alongside emerging and arginine. solubility and
techniques to improve the functionality to the maximum extent. Heat interfacial
assisted pH-shift improved gelling in sunflower protein (Malik & Saini, properties;
2019) and emulsification in coconut protein (Ma et al., 2022). Ultra improved foaming
ability.
sound is the most common technique combined with pH shift. Almost all
Chymotrypsin Next to Least degree of Pea
such studies showed improved solubility and high emulsification hydrophobic amino protein
behavior; studies reported modifications under this domain for plant acids such as hydrolysis.
proteins from amaranth, coconut milk, faba bean, pea, perilla, soy and tryptophan or
rice (Table 3). Following this trend, combining pH shift with advanced phenylalanine.
Transglutaminase Side chain of free Modifies Pea, mung
techniques such as HHP and complexation (protein–polyphenol conju
(most preferred amine group of composition, bean
gation) are emerging (Tan et al., 2021; Yan et al., 2021; Zhou et al., enzyme for protein- or peptide- structure and
2020). cross-linking) bound lysine and conformation of
the γ-carboxamide proteins improve
group of protein- or the emulsifying
5.2.2.2. Non-additive chemical modification. Deamidation: Deamida
peptide-bound ability.
tion increases a protein’s negative charge by converting the amide glutamine.
groups of glutamine and asparagine residues into carboxyl groups. It is Papain Amino acids with Surface-active Peanut, chia
applicable for cereals and legumes with high glutamine and asparagine aromatic side peptides with seed, lupin and
chains. improved oat bran
content and can be done under mild circumstances without chemicals.
solubility and
Acid, alkali, enzyme, and cation-exchange-resin treatments can deami bioactivity,
date, with acid being the most common and alkali the least. Deamida especially
tion minimizes allergenicity, grittiness, bitterness, and lumpiness. antioxidant
Glycation and deamidation improves the flavor profile, solubility, activity.
Pepsin Next to Produce relatively Faba bean
emulsifying, and foaming abilities while decreasing the beany flavor,
hydrophobic amino more hydrophobic
which advocates its use as a component in new food formulations acids such as peptides than
(Nikbakht Nasrabadi et al., 2021). Unfortunately, a dearth of recent tryptophan or trypsin (due to the
literatures pertaining to the deamidation of plant-based proteins has phenylalanine. solubilization of
hydrophobic
been observed.
amino acids);
increase in
5.2.3. Biological modification surface-active
The biological modification techniques entail enzymatic modifica properties.
tion and fermentation. These methods can increase nutritional quality Alcalase Amide bonds. Release the Rice, okara
internal
by modulating protein functionality, digestibility, bioavailability, anti
hydrophobic
oxidant, and antibacterial characteristics. However, enzymes and cul amino acids, and
tures are expensive for large-scale applications. promote
interactions
between them to
5.2.3.1. Enzymatic modification. One of the common approaches in
form aggregates
incorporating proteins into food systems is enzymatic modification, as during heating
the reactants and byproducts of this mild modification are non-toxic. Flavourzyme Hydrophobic Expose the amino Rice, okara
Enzymatic modification, which is quick and highly specific, preserves amino acids and acids located at
peptides at N or C the protein C and
the protein’s original chemical structure in contrast to chemical modi
terminus. N terminals; high
fication. This technique transforms proteins via enzymatic crosslinking degree of
and hydrolysis. Crosslinking occurs when the ɣ-carboxamide group of hydrolysis;
protein-bound glutamine transfers to the lysine via an enzymatically produces peptides
catalyzed acyl transfer process, while hydrolysis is achieved through the with low
bitterness.
enzymatic cleavage of peptide bonds. Hydrolyzing protein increases
ionizable groups and exposes hidden hydrophobic regions (Nikbakht Data extracted from: (Chen & Campanella, 2022; Nikbakht Nasrabadi et al.,
2021).
16
other enzymes (Xu et al., 2021; Zheng et al., 2019) and improved gel led to an increase in the protein’s solubility. The rate of protein ab
strength with mild heating (Chen & Campanella, 2022). Antioxidant sorption into the interface increased, which resulted in the formation of
levels and other functional properties like water binding ability, emul a thick viscoelastic interfacial film, which in turn led to a high emulsi
sification and foaming were also improved (Mulla & Ahmed, 2019). fying ability (Mahdavian Mehr & Koocheki, 2020). Soy protein unfolded
Trypsin hydrolysis resulted in the modification of structure and on exposure to high-energy DBD plasma (18 and 20 kV); this led to the
improved the interfacial film strength, thereby ameliorating the emul formation of intramolecular hydrogen bonds which caused protein ag
sification behavior (Klost & Drusch, 2019). US- and HHP-assisted gregation through intermolecular interactions. The reactive oxygen and
enzymatic treatment of proteins ended up with high degree of hydro nitrogen species produced during the plasma treatment reacted with the
lysis, bioactive peptide yield and improved bioactivity in rice and flax protein and modified its techno-functional properties. An effect of the
seed (Ding et al., 2022; Franck et al., 2019). All the hydrolysates had a state of protein that is subjected to plasma treatment also matters: dry
reduced molecular weight and exhibited better functional characteris proteins have more mechanical distortion due to the effect of corona
tics and bioactivity than the original protein. wind, while aqueous proteins only have chemical changes that would
take part (Sharafodin & Soltanizadeh, 2022). Cold plasma has been
5.2.3.2. Fermentation. Fermentation has proven a cost effective and found to be a promising technique, however, based on the research done
energy efficient biological approach for plant protein modification. It so far, to have a protein modification using cold plasma without any
alters the primary and other higher structural levels of proteins. Lactic significant detrimental effects, optimum power level at less time would
acid bacteria, yeast, mold, and Bacillus strains have all been employed as be recommended. More research is required to understand the reactive
starter cultures for the fermentation of plant proteins, with lactic acid species, its life, effects, resulting interactions and toxicity with food, and
bacteria being the most prevalent. Literature reports improved protein the efficiency of plasma in safe protein modification studies.
solubility, digestibility, nutritional value, bioactivity, foaming, oil and
water holding abilities, decreased beany or off-flavors, bitterness, 6.2. Complexation
allergen or anti-nutrient in soy, chickpea, lupin, and peanut (Nikbakht
Nasrabadi et al., 2021). Further, fermentation of legume seeds increased Proteins are chemically diverse which facilitates them to engage in
the levels of peptides, free amino acids, γ-aminobutyric acid (GABA) molecular interactions such as van der Waals forces, hydrogen bonding,
concentrations, phenols, flavonoids and antioxidants with notable steric repulsion, electrostatic, hydrophobic, and disulfide bridges with a
decrease in oligosaccharides (Arbab Sakandar et al., 2023). Employing variety of chemical compounds, enabling them to create micro-, nano-
fermentation for plant protein modifications requires more attention, and new bio-particles with enhanced flexibility, and techno-functional
and recent studies in this area is quite limited. stability. Hence, there is a growing interest in the process of complex
ing plant-based proteins with other proteins or substances, such as
6. Innovations in protein modification protein-polysaccharide, protein–protein, protein–phenolic, and protein-
surfactant interactions (Pavani, Singha, & Singh, 2024). Table 5. pre
6.1. Cold plasma sents the various molecular interactions involved in the complexations
and the factors that promote their modification.
Plasma treatment can be analogous to PEF, where the highly reactive Scientific studies reported on these complexations revealed that the
oxygen species result in oxidation of proteins that cleave the peptide complexes formed has modified its conformation and structure,
bonds, ending up in structural and functional modifications with improved solubility, stability (mechanical, pH, photo and thermal) and
reduced allergenicity. Excessive exposure to plasma causes over other techno-functional properties, bioactivity, nutritional value,
oxidation and formation of aggregates through intermolecular in encapsulation efficiency, induced delayed gastric digestion and in vitro
teractions. Applying cold plasma to proteins can effectively initiate release and reduced bitterness (Nikbakht Nasrabadi et al., 2021). Poor
surface etching reactions on the protein surface due to the action of high- functionality of pea protein was modified by conjugating it with high
energy reactive species, thereby revealing the active sites. This ulti methoxyl pectin by increasing its solubility (Lan et al., 2018). Glycation
mately leads to an increase in the affinity between the protein and water frequently accompanies the process of protein-polysaccharide conjuga
molecules. The increase of surface polarity in protein molecules is tion. For example, rice proteins were glycated with D-xylose (Jia et al.,
intricately linked to enhanced solubility (Zhang et al., 2020; Zhang 2022) and rapeseed with dextran (Wang et al., 2018). Emulsions formed
et al., 2021). with pea protein isolate-gum Arabic conjugates exhibited reduced par
Atmospheric cold plasma has found its application in improving the ticle size, increased surface charge, and improved steric hindrance for
gelation and glycation of pea proteins (Zhang et al., 2021) as well as enhanced emulsion stability against external factors and lipid oxidation
reduction of allergenicity in soy proteins (Zhang et al., 2020). It reduced (Zha et al., 2019). Application of advanced technologies like HHP
the trypsin inhibitor activities in soy and led to improved digestibility (soy protein with flaxseed) and cold plasma (pea protein with
and post-digestion amino acid quantity; the secondary and tertiary dextran) to glycate proteins with polysaccharides are gaining attention
structures of the protein were modified which enhanced the techno- as the conjugates possessed improved functionality (Ji et al., 2020; Liu
functional properties (Dabade et al., 2023). Atmospheric pressure et al., 2020). Cold plasma assisted glycation of poorly soluble peanut
plasma also enhanced the emulsification and foaming of wheat germ protein obtained from high temperature pressed peanut flour, an in
protein isolate when subjected at alkaline pH for less time (5 min). dustrial by-product, with lactose improved its solubility, ordered
Nevertheless, prolonged exposure (40 min) of protein to plasma structure and thermal stability (Yu et al., 2020). Such synergistic mod
increased its solubility and WHC, but altered its morphology (Abarghoei ifications open a new way for by-product utilization and their applica
et al., 2023). Similar improvement in functionality was obtained for tions in food.
flaxseed protein, with less exposure time; additionally, there was release The process of protein–polyphenol conjugation is commonly
of phenols, flavanols and antioxidants; while, with increase in exposure employed for the purpose of encapsulation, wherein the preservation of
time—there was an increase in oxidation of these phenols, particle size the bioactive constituent (polyphenol) is necessary until its subsequent
(leading to poor solubility) and surface hydrophobicity and drop in release. This process can be facilitated by conjugating it with protein via
antioxidant activity (Yu et al., 2020). covalent or non-covalent interactions, such as van der Waals forces and
The high-energy dielectric barrier discharge (DBD) cold plasma hydrophobic interactions. The former type of interactions leads to the
resulted in cleaving of the covalent bonds of grass pea (Lathyrus sativus formation of complexes that exhibit high heat stability, anti-digestive
L.) and caused secondary structure modifications; reduced particle size properties, and protection against oxidation through polyphenol pres
ervation. On the other hand, the latter type of interactions enhances the
17
Table 5
Interactions during plant protein complexation and their promoting factors.
Complexation Interaction Promoting factor Reference
Protein- Electrostatic interaction pH (Warnakulasuriya &

polysaccharide Nickerson, 2018)
Protein-protein Hydrogen bonding and hydrophobic reactions Heat, high-pressure and enzymatic hydrolysis (Zheng et al., 2020)
Protein-phenolic Covalent and non-covalent bonding (reversible − hydrogen and pH, free radical mediated grafting, enzyme (Yan et al., 2021); (Zhou
hydrophobic bonding, van der Waals forces and electrostatic catalyzed grafting and chemical coupling methods et al., 2020)
interactions)
Protein-surfactant Electrostatic and hydrophobic interactions Heat, pH, salt (Nikbakht Nasrabadi et al.,
2021)
binding of conjugate components, its bioactivity and bioavailability. It ‘amyloid’ or ‘nanostructured’ status (Cao & Mezzenga, 2019). There
was observed that an alkaline pH serves as a facilitative factor in this fore, it is crucial to thoroughly evaluate the safety of amyloid fibrils
kind of complexation, owing to its capacity to induce structural modi individually, taking into account factors such as the conditions in which
fications and unleash the sulfhydryl groups (Yan et al., 2021; Zhou et al., they form, the structure, the source of the protein, and the characteris
2020). This form of complexation is found in soy protein with tics of the food matrix in which they will be dispersed and distributed.
epigallocatechin-3-gallate or EGCG (Yan et al., 2021; Zhou et al., 2020)
and cyanidin-3-O-glucoside (Chen et al., 2019), rice protein with 7. Impact of protein modifications on nutrition
anthocyanin (Li et al., 2020), and rice-pea protein blend with poly
phenols from berry and grape pomace (Xiong et al., 2020). A protein’s nutritional excellence is assessed by considering its bio
logical value, digestibility, amino acid profile, essential amino acid
6.3. Amyloid fibrillization composition, net protein utilization, purity, protein digestibility-
corrected amino acid score (PDCAAS), and antinutritional factors
This is not a new technique, but it is gaining significant attention in (Pam Ismail et al., 2020; Sá et al., 2020b). Understanding the complete
protein modification in the recent years. Protein amyloid fibrils are nutritional constitution of proteins is vital for developing products from
aggregates of protein formed under specific conditions such as low pH, them, particularly when working with alternative protein sources. As
low salt, and high temperatures (70–90◦ C), which result in partial previously mentioned, plant proteins are deficient in certain amino
unfolding or hydrolysis of proteins. This assembly occurs through the acids. Therefore, a proper combination of plant-based proteins or related
interaction of amino acid sequences prone to fibrillization through the diets will offer an ideal balance of the necessary amino acids required for
intermolecular stacking of β-sheets. The formation of amyloid fibrils is physiological function (Akharume et al., 2021). Preserving the nutri
an inherent characteristic exhibited by all proteins. β-strands of protein tional value is crucial when focusing on enhancing the functionality of
serve as the precursors of β-sheets; and these β-sheets arrange them protein.
selves into a cross-β structure, parallel to the fibril axis with 4.8 Å inter- Protein modifications leads to alterations in the molecular structure,
strand distance and 6 ~ 12 Å inter-sheet distance. This cross-β structure which affect the functionality of proteins and the overall quality of food
extends into protofilaments, which then twist together to form multi- products. Concurrently, changes in the chemical composition take place,
stranded mature helical amyloid fibrils (Cao & Mezzenga, 2019). The ultimately altering the protein’s nutritional value and its accessibility in
improved structural and functional stability, and techno-functional at the gastrointestinal system (Akharume et al., 2021). Research on plant
tributes created opportunities to exploit their distinctive physicochem proteins revealed that they are more resistant to human digestion than
ical and nanomechanical characteristics in food industry as emulsifiers, animal proteins since they possess more β-sheet structures and
thickeners, stabilizers, gelling agents, antimicrobials, encapsulation, comparatively fewer α-helixes. Another factor contributing to the
and drug delivery agents. Temperature, pH, salt and protein concen reduced proteolytic digestibility of plant-based proteins is the higher
trations, agitation, and degree of unfolding all have a significant impact concentration of fibers that compose the plant foods. In addition to this,
on the molecular arrangement of amyloid fibrils (Kutzli et al., 2023). they are not as easily assimilated by the human digestive system as
Stable soy protein amyloid fibrils was formed at 85◦ C with hydrolytic animal-based proteins due to the presence of antinutritional factors,
heating for 8–10 h and incubation for 3 days; these fibrils demonstrated which hinder the absorption of nutrients from ingested food (Sim et al.,
superior gelling performance and produced stronger gels compared to 2021). The nutritional value of proteins can be improved by increasing
the non-fibril proteins (Wang et al., 2020). However, heating at the same the protein digestibility and bioavailability by reducing the ANFs and
conditions for 24 h enhanced the β-folded structures to 53.61% with protein allergenicity (Avelar et al., 2021).
increase in emulsifying behavior and viscosity (Yu et al., 2024). The Conventional modification techniques such as heat (cooking, auto
mechanism of formation of amyloid fibrils is different for different claving, extrusion), germination and fermentation help in inactivating
proteins, and predominantly depends on the ability to form fibrils. This the ANFs that impair with nutrient absorption (Sá et al., 2020a). How
can be evident from the amyloid fibrillization of legumes such as ever, thermal processing at high temperatures can impair the nutritional
cowpea, lentils and chickpea which showed that vicilin rich cowpea and sensory properties of a protein, leading to the formation of unde
protein had the highest fibril forming ability with long and flexible sirable compounds with loss of its bioactivity. On the other hand, the
nature, possessed better rheological properties than lentil and chickpea advent of novel thermal processes such as irradiation, microwave and
that formed semiflexible and rigid fibrils respectively (Li et al., 2021). ohmic heating has very low or no detrimental impact on nutrition while
Another recent work reported that amyloid fibrillization of hempseed improving the digestibility and reducing allergenicity (Dash et al., 2022;
protein improved its protein solubility (Kutzli et al., 2023). Amaranth Mathews et al., 2023; Nikbakht Nasrabadi et al., 2021). In case of
germ meal proteins are rich in β-sheets and showed mesoscopic poly chemical modifications, they generate toxic and allergenic substances
morphism with rigid amyloid fibrils (Mykolenko et al., 2024). that have a detrimental impact on the nutritional value and are not
Currently, despite the abundance of evidence suggesting that food conducive to health (Dash et al., 2022).
protein fibrils are safe to consume, understanding the fate of food pro Non-thermal techniques such as ultrasound induces acoustic cavi
tein amyloids along the gastrointestinal tract and their potential toxicity tation, which potentially reduces the ANFs and affect their allergenic
is still inadequate. Ensuring the safety of amyloid fibrils is a fundamental properties (Sengar et al., 2022). Application of ultrasound was prom
requirement for the success of all these applications in food, due to their ising for improving the digestibility of proteins from amaranth, potato,
18
sesame (Figueroa-González et al., 2022; Hussain et al., 2021; Mathews phenomenon promotes the formation of a three-dimensional lattice,
et al., 2023). High pressure is equally effective in modifying the func thereby giving rise to a gel structure (Avelar et al., 2021). Based on the
tionality as well as improving the digestibility of proteins; this was review conducted (Table 3), there is always a positive correlation be
evident from the improved nutritional value of proteins from soy, split tween the WHC and gelation of proteins (Chen & Campanella, 2022; J. Li
pea, soursop, red bean, kidney bean, and flaxseed (Avelar et al., 2021; et al., 2020; Malik & Saini, 2018, 2019; Mathews et al., 2023; Mir et al.,
Villacís-Chiriboga et al., 2023). Other emerging techniques such as 2020; Nisov et al., 2020; Shah et al., 2019; Wang et al., 2018; Zhang
pulsed electric field and moderate electric field also showed to et al., 2021), except for the turtle bean protein modified by pH shift and
improvement in the digestibility of proteins (Mathews et al., 2023). sesame protein modified by microwave (He et al., 2020; Mathews et al.,
However, there is a need for extensive investigations to enhance our 2023).
understanding of nutritional improvement through techniques such as
cold plasma and complexation. 9. Concluding remarks and recommendations
8. Interrelationships in plant protein functionality This review focuses on the recognition and comprehensive study of
novel plant protein sources, with the aim of gaining a thorough under
The techno-functional characteristics of plant proteins consists of standing of their characteristics and exploring their potential applica
solubility, water and oil/fat holding capacities, gelling, emulsifying and tions in food. The pre-extraction treatment is of utmost importance as it
foaming abilities and foam stability. These traits play a crucial role in significantly impacts the protein yield, purity, and, in certain instances,
determining the behavior of plant proteins within the food systems. The the functionality. The strategic use of cold pressing as a pretreatment
functionality of proteins is contingent upon both their intrinsic attri method is suggested as the most effective approach for improving both
butes, such as conformation, structure, and amino acid composition, as the quantity and quality of protein extraction. It is imperative for
well as the external elements that influence them, for example temper extraction studies to provide extensive details regarding the specific
ature, pH, and ionic strength. protein fractions and the potential presence of antinutrients within the
The assessment of protein solubility holds significant importance as extracted protein. This piece of information will prove invaluable to
it is intricately linked to other vital functional attributes, including researchers and the wider scientific community, as it will enhance their
gelling, emulsifying, and foaming abilities, and potential food applica understanding of proteins and facilitate the exploration of potential
tions. Protein extraction employs diverse solvents and during precipi methods for their functionalization and utilization in the food industry.
tation, at the pI, there will be an equilibrium of positive and negative Furthermore, it advances the potential for the commercialization of the
charges that reduces the electrostatic forces, resulting in aggregation protein, as endorsed by regulatory bodies.
(Novák & Havlíček, 2016). Thus, protein solubility greatly relies on the The evolution from chemical to physical methodologies for the
surface charge, balance of hydrophobic-hydrophilic groups in the pro extraction and modification of plant proteins has been a notable tran
tein structure, and the solution type, pH, temperature, and ionic sition in the realm of scientific research. This shift signifies a transition
strength. Almost all of the reviewed literatures estimated the solubility from traditional chemical-based approaches towards more advanced
of protein upon modification. This stresses the indispensable role of and sophisticated physical techniques. Such a progression has been
solubility in determining protein functionality. Plant protein solubility driven by a desire to enhance the efficiency, precision, and sustainability
improved with all the modification methods except for some cases of protein extraction and modification processes. By harnessing the
(Table 3). power of physical techniques and its combination with other methods,
Water holding capacity (WHC) unveils the ability of protein to hold researchers have been able to open new avenues for modifying plant
water and is associated with the presence of polar amino acids in proteins, thereby broadening their scope in the development of designer
protein-water interaction sites, while oil holding capacity (OHC) is the foods and other novel functional food systems.
ability of protein to absorb fat or oil and is determined primarily by the Contemporary research to simultaneously extract and modify plant
presence of nonpolar amino acids in protein-oil interaction sites. Both proteins focuses through the utilization of cutting-edge methods such as
WHC and OHC components play a pivotal role in researching and ultrasound, microwave, pulsed- and moderate-electric field, from novel
developing plant-derived meat substitutes and viscous food products, as plant protein sources. Ultrasound has emerged as a highly promising
they are vital determinants of food texture and flavor retention (Avelar technique to achieve optimal protein extraction along with improving
et al., 2021). These properties are not always determined; they are protein quality. Other techniques are quite emerging and require more
mostly evaluated when novel proteins or novel modifications are under research. Plant protein modifications are promising, as they can be
research, or when its complementary attributes are studied. focused on specifically improving certain attributes such as solubility,
Emulsions and foams are created when oil droplets disperse in an emulsification, and gelation of plant proteins. The application of
aqueous medium or when air cells are covered in a film. The inherent advanced techniques, such as high-pressure processing, cold plasma
capacity of proteins to undergo adsorption at the interface of oil or air treatment, protein conjugation and complexation with other bio mac
droplets facilitates the formation of stable films and dispersions, thereby romolecules, and amyloid fibrillization, has demonstrated a significant
serving as emulsifying and foaming agents. Emulsification ability is impact on the functional properties of modified plant proteins. For
often associated with the OHC, where an increase in emulsification nutritional betterment of plant proteins, ultrasound, high pressure and
behavior is observed for proteins with good OHC (Table 3). A correlation radiative techniques were found promising. Further, the interrelation
can be said to exist between the surface charge of proteins and its ship in functionality requires intensive studies, particularly when there
foaming ability, as a greater charge lowers the hydrophobic interactions, is a need to improve a specific functional attribute. Nevertheless, these
leading to an enhancement in the solubility of proteins, enabling them to alterations are currently limited to research at a lab scale and would
disperse rapidly on the interface and trap the air bubbles (Avelar et al., necessitate approval from the government and regulatory bodies before
2021). This statement is supported by this review (Table 3) which shows they can be implemented in the food industry.
that increasing foaming ability is always accompanied with an increase
in solubility with very few exceptional cases. 10. Future prospects
When proteins unfold, their hydrophobic amino acid residues are
exposed, leading to the formation of attractive forces between the Plant-based diets are now a global trend; to be precise, the plant-
nonpolar regions of different proteins. These forces and their in based milk, protein and meat analogs are attracting major attention
teractions are stabilized by the intermolecular forces and interactions, among consumers. Although many protein sources were discussed, in
which may lead to irreversible aggregation. The proliferation of this light of the booming demand, pressing concerns of sustainability, and
19
principles of circular bioeconomy, it would be prudent to direct our References

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Food Research International 190 (2024) 114575

Contents lists available at ScienceDirect

Food Research International

A comprehensive review on the recent trends in extractions, pretreatments

Food Research International 190 (2024) 114575

Food Research International 190 (2024) 114575

Fig. 1. Classification of protein extraction techniques.

*AE/IP: Alkaline Extraction followed by Isoelectric Precipitation

Amaranth Alkaline pH shift þ þ ¡ þ þ Alkaline pH shift with US caused notable (Figueroa-

Protein- þþ þ ¡ þ ¡ Controlled Maillard reaction (glycated (Zha et al., 2019)

Protein- Electrostatic interaction pH (Warnakulasuriya &

principles of circular bioeconomy, it would be prudent to direct our References

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