Vegetable Proteins in Microencapsulation: A Review of Recent Interventions and Their Effectiveness

Industrial Crops and Products 42 (2013) 469–479
Contents lists available at SciVerse ScienceDirect
Industrial Crops and Products

journal homepage: www.elsevier.com/locate/indcrop
Review
Vegetable proteins in microencapsulation: A review of recent interventions and

their effectiveness
Alla Nesterenko a,b , Isabelle Alric a,b , Françoise Silvestre a,b , Vanessa Durrieu a,b,∗
a
Université de Toulouse, INP-ENSIACET, LCA (Laboratoire de Chimie Agro-industrielle), F-31030 Toulouse, France
b
INRA, UMR 1010 CAI, F-31030 Toulouse, France
a r t i c l e i n f o a b s t r a c t
Article history: Proteins from vegetable seeds are interesting for research at present because they are an abundant
Received 3 April 2012 alternative to animal-based sources of proteins and petroleum-derived polymers. They are a renew-
Received in revised form 19 June 2012 able and biodegradable raw material with interesting functional and/or physico-chemical properties. In
Accepted 22 June 2012
microencapsulation, these biopolymers are used as a wall forming material for a variety of active com-
pounds. In most cases, two techniques of microencapsulation, spray-drying and coacervation, are used
Keywords:
for the preparation of microparticles from vegetable proteins. Proteins extracted from soy bean, pea and
Vegetable proteins
wheat have already been studied as carrier materials for microparticles. These proteins could be suit-
Microencapsulation
Soy proteins
able shell or matrix materials and show good process efficiency. Some other plant proteins, such as rice,
Pea proteins oat or sunflower, with interesting functional properties could be investigated as potential matrices for
Spray-drying microencapsulation.
Coacervation © 2012 Elsevier B.V. All rights reserved.
Contents
1. Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 470
2. The microencapsulation techniques applied to vegetable proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 471
3. Vegetable proteins in microencapsulation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 471
3.1. Soy proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 471
3.1.1. Microencapsulation by spray-drying . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 471
3.1.2. Microencapsulation by coacervation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 473
3.2. Pea proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 473
3.2.1. Microencapsulation by spray-drying . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 473
3.2.3. Pea proteins as an additive for microencapsulating systems . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 474
3.3. Wheat proteins and other cereal proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 474
3.3.2. Microencapsulation using other processes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 475
3.4. Other vegetable proteins potentially useful in microencapsulation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 475
3.4.1. Rice proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 475
3.4.2. Oat proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 476
3.4.3. Sunflower proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 476
4. Industrial applications of microencapsulation by vegetable proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 477
5. Conclusions and future prospects . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 477
References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 477
∗ Corresponding author at: Université de Toulouse, INP-ENSIACET, LCA (Laboratoire de Chimie Agro-industrielle), F-31030 Toulouse, France.
Tel.: +33 5 34 32 35 09; fax: +33 5 34 32 35 97.
E-mail address: [email protected] (V. Durrieu).
0926-6690/$ – see front matter © 2012 Elsevier B.V. All rights reserved.
http://dx.doi.org/10.1016/j.indcrop.2012.06.035
470 A. Nesterenko et al. / Industrial Crops and Products 42 (2013) 469–479
Fig. 1. Different morphologies of microparticles obtained by microencapsulation: (a) microcapsule, (b) microsphere, (c) multilayer microcapsule and (d) multishell and
multicore microsphere.
1. Introduction et al., 2005; Saénz et al., 2009; Semyonov et al., 2010), gum Ara-
bic (Kim et al., 1996; Shaikh et al., 2006), pectin (Drusch, 2007;
Microencapsulation consists of the isolation of active substances Gharsallaoui et al., 2010), chitosan (Higuera-Ciapara et al., 2004;
(in the liquid, solid or gas state), to obtain products with spherical Pedro et al., 2009), and alginates (Yoo et al., 2006; Huang et al., 2010;
form and micrometric size, in which the active material or core, Wikstrom et al., 2008). The major advantages of these biopolymers
is shielded by a membrane from the surrounding environment. are their good solubility in water and low viscosity at high con-
This technique can be applied for different purposes: protect- centrations, compared to proteins. Often carbohydrates are mixed
ing sensitive substances from the surroundings, development of with proteins (Augustin et al., 2006; Ducel et al., 2004b; Mendanha
controlled release properties, masking of unpleasant taste and et al., 2009; Pereira et al., 2009; Pierucci et al., 2006, 2007; Yu
odor of the substances, dilution of core material when it must et al., 2007) to improve the emulsifying and filmogenic properties
be used in very small amounts or transformation of liquid com- during microencapsulation. Furthermore, protein–carbohydrate
pounds into mobile solids. Microencapsulation allows the creation conjugates covalently cross-linked by the Maillard reaction had
of a physical barrier between the core and wall materials and the shown interesting functional properties (Augustin et al., 2006; Rusli
protection of sensitive ingredients (flavors, antioxidants, polyun- et al., 2006). Various lipophilic substances such as glycerides, oils,
saturated oils, vitamins, drugs, etc.) from the external medium, phospholipids, carotenoids and waxes are also used as carrier mate-
particularly, moisture, pH and oxidation. The release of micropar- rials in microencapsulation (Eldem et al., 1991; Lee et al., 2003;
ticle content at controlled rates can be triggered by shearing, McClements et al., 2007; Muller et al., 2002; Patel et al., 2010). They
solubilization, heating, pH or enzyme action. This technology has permit barrier creation for the protection of sensitive ingredients
different applications in the food, biomedical, pharmaceutical and against moisture, plus their transport in aqueous media.
cosmetic industries as well as in agriculture and catalysis (Dubey Proteins extracted from animal derived products (whey pro-
et al., 2009). The structure of microparticles is generally classi- teins, gelatin, casein) and from vegetables (soy proteins, pea
fied into microcapsules with a single core surrounded by a layer proteins, cereal proteins) are widely used for encapsulation of
of wall material; microspheres with the core dispersed in a con- active substances. These natural polymers present several advan-
tinuous matrix network and more complex structures such as tages: biocompatibility, biodegradability, good amphiphilic and
multilayer microcapsules or multishell microspheres (Fig. 1). Var- functional properties such as water solubility, and emulsifying and
ious processes may be used to produce encapsulated ingredients foaming capacity. The use of vegetable proteins as wall-forming
(Augustin et al., 2006; Benita, 2006; Dubey et al., 2009; Gouin, 2004; materials in microencapsulation, reflects the present “green” trend
Munin and Edwards-Lévy, 2011; Jyothi et al., 2010): spray-drying, in the pharmaceutical, cosmetics and food industries. In food appli-
spray-cooling/chilling, fluidized bed, coacervation/phase separa- cations, plant proteins are known to be less allergenic compared
tion, gelation, solvent evaporation, supercritical fluid expansion, to animal derived proteins (Jenkins et al., 2007; Li et al., 2012).
interfacial polymerization (polycondensation), emulsion polymer- For these reasons, over the past few years, the development of
ization and extrusion. Choice of microencapsulation technique for new applications for plant products rich in proteins has became
a particular process will depend on the size, biocompatibility and an increasingly interesting area for research. For the last decade,
biodegradability of microparticles needed, the physico-chemical the protein ingredient industry has been turning towards plants
properties of core and coating, the microparticles’ application, the as a preferred alternative to animal-based sources, e.g. in vege-
proposed mechanism for active core release, and on the process tarian diets, due to increased consumer concerns over the safety
costs. of animal-derived products (Jiménez-Yan et al., 2006; Sawashita
Wall material particularly affects the microparticles’ stability, et al., 2006; Choi et al., 2010). Currently, the widespread presence
the process efficiency and the degree of protection of the active of microparticles based on animal proteins, contrasts with the very
core. Materials commonly used as carriers in the makeup of encap- limited use of plant proteins in industry. This tendency should be
sulated ingredients, are synthetic polymers and co-polymers, and reversed in coming years.
bio based materials such as carbohydrates, fats, waxes, and animal Vegetable proteins consist of several fractions: the major frac-
and plant derived proteins. Petroleum derived polymers commonly tion is glutenin, soluble in alkaline water solutions; the globulin
used in pharmacy and medicine as a matrix for microparticle fraction, soluble in salt solutions, followed by the albumin and
preparation are polystyrenes, polyamides, polyurethanes, poly- prolamin, fractions soluble in water and ethanol, respectively
acrylates, phenolic polymers, and poly(ethylene glycols) (Dubey (Osborne, 1909). Among vegetable proteins used as a wall material
et al., 2009). Functionalization of polymeric chains makes it pos- in microencapsulation, we find mainly soy protein isolate, pea pro-
sible to obtain microparticles with new properties, different from tein isolate and cereal proteins. Soybean proteins have functional
those obtained with other wall materials, for example resistance properties suitable for microencapsulation, such as solubility,
to the action of chemical agents (Patel et al., 2010). Polysaccha- water and fat absorption, emulsion stabilization, gelation, foam-
rides studied as a matrix for microencapsulation are starches (Jeon ing, plus good film-forming and organoleptic properties (Franzen
et al., 2003; Murúa-Pagola et al., 2009), maltodextrin (Krishnan and Kinsella, 1976). Soy glycinin and conglycinin are somewhat
A. Nesterenko et al. / Industrial Crops and Products 42 (2013) 469–479 471
similar (comparable molecular weights, amino acid composition, and sensitive to precipitation with pH values lower than 7, espe-
subunit structures) to pea legumin and vicilin (Koyoro and Powers, cially when acidic core materials are used (e.g. ascorbic acid). For
1987). The globulins of pea protein have all the functional proper- the majority of vegetable proteins in aqueous solution, the isoelec-
ties necessary for successful incorporation into microencapsulation tric point is located in a pH range between 3 and 5. For this reason
systems as a wall material. The proteins of cereals (oat, wheat, these biopolymers are usually used in alkaline conditions in order
barley and corn) are more advantageous from the nutritional stand- to obtain good solubility of proteins and to efficiently encapsulate
point, and they have attracted research and commercial attention active substances.
for this reason. Due to their interesting functional properties and Particle properties, such as morphology, size and releasing char-
potential food applications, these proteins were also studied as wall acteristics, can be very different depending on the process chosen.
material for microencapsulation (Ducel et al., 2004a, 2005; Wang Two forms are mainly obtained by the spray-drying and coacerva-
et al., 2011b). Sunflower proteins have particularly interesting ther- tion method: microcapsules and microspheres (Fig. 1). Particle size
mal behavior, gelling properties and surface activity. Compared obtained by the spray-drying process is typically between 1 ␮m and
with other sources of vegetable proteins, sunflower seeds have 50 ␮m (Richard and Benoit, 2000) while size of particles obtained
been reported to have a low content in anti-nutritional factors. by the coacervation method can vary from nanometers to several
These proteins have often been compared to commercial soy pro- hundred microns (Merodio et al., 2001; Bayomi et al., 1998; Gan
teins, extensively researched on functionality, with regard to their et al., 2008).
functional properties (Gonzalez-Perez and Vereijken, 2007). These two processes give high values (up to 100%) of microen-
This review presents the recent works dealing with the use capsulation efficiency (MEE). The latter is defined as the ratio
of vegetable proteins in microencapsulation. The influence of the between the percentage of active core encapsulated in the powder
proteins functional properties as well as the microencapsula- and the percentage of active core in the initial liquid.
tion technique on process efficiency and properties of obtained
microparticles is particularly discussed.
3. Vegetable proteins in microencapsulation
3.1. Soy proteins

2. The microencapsulation techniques applied to vegetable
proteins
Soy bean seeds contain an important fraction (35–40%) of pro-
teins mainly glycinin and conglycin (50–90% of total proteins)
The two techniques mainly used for microencapsulation of
(Ruiz-Henestrosa et al., 2007). The glycinin fraction (11S globulin)
active material by vegetable proteins are spray-drying and coacer-
has a molecular weight of about 350 kDa while conglycin (7S globu-
vation. Both processes share the aspect of “green chemistry” with
lin fraction) is about 70 kDa. Isolated and purified soy proteins show
vegetable proteins as renewable and biodegradable resources, plus,
interesting physico-chemical and functional attributes in particu-
the two techniques do not need the use of organic solvents. Other
lar gel-forming, emulsifying and surfactant properties (Gu et al.,
processes such as gelation or solvent evaporation techniques can
2009). These protein characteristics and their solubility are strongly
be also considered (Dubey et al., 2009; Gouin, 2004).
dependent on pH, heat treatment, and the presence and concentra-
Spray-drying is a continuous process to convert an initial liquid
tion of salts or other ingredients (oil, carbohydrate, surfactant)
into a solid powder of microparticles (Fig. 2a). It is a very common
Soy protein isolate (SPI) use in microencapsulation has already
dehydration process used to form a continuous matrix surround-
been studied by various authors (Table 1). SPI is generally used as an
ing the active substances. The initial liquid (solution, emulsion or
individual coating material, but can also be mixed with polysaccha-
suspension) containing wall and core materials is sprayed into a
rides (Augustin et al., 2006; Rusli et al., 2006; Yu et al., 2007). The
stream of heated air. The solvent, almost always water, is evap-
combination of proteins with carbohydrates as a carrier material
orated to give instantaneous powder production. This technology
favors better protection, oxidative stability and drying properties
offers several advantages: it is simple, relatively inexpensive, rapid
(Augustin et al., 2006). Due to SPI hydrosolubility, microparticles
and thus widely used in industry. The important factor for success-
are mainly produced using the spray-drying technique (Augustin
ful microencapsulation by spray-drying is a high solubility of shell
et al., 2006; Charve and Reineccius, 2009; Favaro-Trindade et al.,
material in water (or other chosen solvent) and a low viscosity at
2010; Kim et al., 1996; Ortiz et al., 2009; Rascon et al., 2010; Rusli
high solid content. Disadvantages of this technique are loss of a sig-
et al., 2006; Yu et al., 2007), but coacervation and gelation have also
nificant amount of product (due to adhesion of the microparticles
been investigated (Chen and Subirade, 2009; Gan et al., 2008; Lazko
to the wall of the spray-dryer) and the possibility of degradation of
et al., 2004a,b; Mendanha et al., 2009; Nori et al., 2010).
sensitive products at high drying temperatures.
Microencapsulation by coacervation is carried out by precipi-
tation of wall forming materials around the active core under the 3.1.1. Microencapsulation by spray-drying
effect of one of the following factors: change of pH or temperature, In the case of hydrophobic core microencapsulation, an oil-
addition of a non-solvent or electrolyte compound (Fig. 2b). This in-water emulsion is prepared before the encapsulation step
controlled desolvation results in the formation of a polymeric net- (Augustin et al., 2006; Kim et al., 1996; Rascon et al., 2010;
work around the core. This shell of coacervates can be solidified Rusli et al., 2006; Yu et al., 2007; Nesterenko et al., 2012). These
using a chemical or enzymatic cross-linker (Gouin, 2004). Coac- emulsions are often carried out by high pressure homogenization
ervation occurs either via a simple or complex method. Simple because of its interesting results in terms of emulsion proper-
coacervation involves only one colloidal solute and thus formation ties and stability (Gharsallaoui et al., 2007). Moreover, increasing
of a single polymer envelope. Complex coacervation is produced by homogenization pressure gives a slight decrease in oil droplet size
mixing two oppositely charged polyelectrolytes for shell formation (Rusli et al., 2006) and emulsion viscosity (Yu et al., 2007). Rusli
around an active core (Wilson and Shah, 2007). Finally, one of the et al. (2006) also noted a slight improvement in microencapsula-
factors that limits the use of coacervates in encapsulation is their tion efficiency with an increase of homogenization pressure. Some
sensitivity to pH and ionic strength (Augustin et al., 2006). results are given in Table 2.
The important point to consider for the use of proteins in encap- The intense mechanical forces undergone by globular proteins
sulation systems is their instability in acid media. The isoelectric and oil droplets during homogenization, promotes oil droplet dis-
point of proteins means they are insoluble in most acidic systems persion and protein structure modification (Rampon et al., 2003),
Fig. 2. Schematic representation of microencapsulation process by spray-drying (a) and coacervation (b) techniques.
Redrawn from Jyothi et al. (2010).
Table 1
Microencapsulation with SPI-based wall material.
Microencapsulation process Wall material Core material Reference
Spray-drying SPI Orange oil Kim et al. (1996)

Spray-drying Mixture of proteins and polysaccharides Fish oil Augustin et al. (2006)
Spray-drying SPI/glucose syrup Stearin, palme oil Rusli et al. (2006)
Spray-drying SPI/maltodextrin Phospholipide Yu et al. (2007)
Spray-drying SPI Flavors Charve and Reineccius (2009)
Spray-drying SPI Casein hydrolysate Ortiz et al. (2009)
Spray-drying SPI Paprika oleoresin Rascon et al. (2010)
Spray-drying SPI/gelatin Casein hydrolysate Favaro-Trindade et al. (2010)
Spray-drying SPI ␣-Tocopherol Nesterenko et al. (2012)
Simple coacervation SPI Fish oil Gan et al. (2008)
Simple coacervation Soy glycinin Hexadecane Lazko et al. (2004a)
Complex coacervation Soy glycinin/sodium dodecylsulfate Hexadecane Lazko et al. (2004b)
Complex coacervation SPI/pectin Casein hydrolysate Mendanha et al. (2009)
Complex coacervation SPI/pectin Propolis Nori et al. (2010)
Complex coacervation SPI/gum Arabic Orange oil Jun-xia et al. (2011)
Gelation SPI Riboflavin Chen and Subirade (2009)
such as unfolding of proteinic chains. This unfolding causes the hand, past a critical concentration (generally 20% (w/w) solid con-
exposure of polar and non polar protein regions, and movement of tent) an abrupt increase in viscosity is observed, which involves a
charged amino acids to new local environments and makes them significant fall in process efficiency (Yu et al., 2007).
more surface-active. The main changes are in the secondary and ter- From the process point of view, it has been shown that drying
tiary structure that can modify the surface appearance of the amino inlet temperature also affects the MEE. Indeed, a high drying tem-
acids. As proteins are the most surface-active components in the perature supports the formation of a rigid wall material shell on the
emulsion they accumulate at the oil–water interface, enwrapping microparticle surface, limiting core molecule migration and release
the newly formed oil droplets. This can be explained by the ten- (Rascon et al., 2010).
dency of proteins to adsorb more extensively and less reversibly In the spray-drying microencapsulation process, efficiency can
at hydrophobic surfaces than at hydrophilic surfaces (Dickinson, also be influenced by volatile properties of active core material, e.g.
1999). The resulting stabilizing layer provides immediate protec- a decrease of MEE for encapsulation of volatile composites such
tion of the fine droplets against re-coalescence and thus gives as aromas compared to classic oils. Indeed, during the drying pro-
physical stability to the emulsion (Dickinson, 2001). cess, the liquid preparations are subjected to high temperatures
The solid level in the emulsion is also a key parameter influ- (150–180 ◦ C) and this provokes core material evaporation, which
encing active core retention (Charve and Reineccius, 2009), and it explains the low efficiency of microencapsulation of citral (35%)
has been shown that the MEE is improved with increasing solid (Charve and Reineccius, 2009) compared to stearin (91%) (Rusli
content. This could be explained by the reduction of core molecule et al., 2006) by SPI.
mobility in wall material and of the time needed to form the pro- In our recent study (Nesterenko et al., 2012), it has been shown
tective shell, both induced by a high solid content. On the other that grafting of hydrophobic fatty acid chain to soy proteins by
Table 2
High pressure homogenization influence on the SPI-based emulsions properties.
Wall/core (w/w) Pressure (MPa) Droplet size (␮m) Viscosity (cP) Reference
2/1 35 1.52 – Kim et al. (1996)

2/1 35 0.57 ± 0.1 – Augustin et al. (2006)
1/1 18 → 35 0.45 → 0.32 – Rusli et al. (2006)
1/1 15 → 55 – 100 → 70 Yu et al. (2007)
4/1 30 1.05 ± 0.66 – Rascon et al. (2010)
2/1 50 1.1 ± 0.02 15 Nesterenko et al. (2012)
acylation can enhance the retention of hydrophobic active mate- In an effort to mask the bitter taste of some hydrophobic
rial (␣-tocopherol) during microencapsulation by spray-drying. hydrolysates (e.g. casein hydrolysate) and be able to incorporate
Process efficiency was improved from 79.7% to 94.8% when soy them into food products, their microencapsulation by soy pro-
proteins were acylated with dodecanoyl chloride. Moreover, this teins was investigated by spray-drying (Favaro-Trindade et al.,
increased retention efficiency after protein acylation was observed 2010; Ortiz et al., 2009) and coacervation (Mendanha et al., 2009)
for different core/wall ratios, demonstrating that soy proteins in techniques. During encapsulation, the hydrophobic interactions
native and modified state represent a relevant encapsulant agent between casein hydrolysate and soy proteins lessen the undesirable
for hydrophobic substances. taste of casein. In both cases, the authors demonstrate the decrease
in microencapsulation efficiency and the increase in particle size
with increasing active core concentration.
3.1.2. Microencapsulation by coacervation Chen and Subirade (2009) reported the preparation of soy pro-
Soy proteins have also been studied in microencapsulation as tein based microspheres by cold gelation method (initiated by
wall materials using the coacervation method, and several param- glacial acetic acid in the presence of calcium carbonate) to elaborate
eters influencing the coacervation MEE have been found. Among delivery systems for nutraceutical products (riboflavin). Obtained
them: the active core and wall material concentrations, the tem- microparticles had spherical morphology with the diameter about
perature and the pH of the media. When active hydrophobic core 15 ␮m. Active material was efficiently encapsulated by soy proteins
concentration exceeds 50% (w/w), a decrease in process efficiency (process efficiency of 79–88%) at ambient temperature without
is generally observed (Lazko et al., 2004a; Mendanha et al., 2009; using cross-linking reagents, which could be interesting for various
Rusli et al., 2006; Jun-xia et al., 2011). This phenomenon is particu- food and pharmaceutical applications.
larly well illustrated in the work of Mendanha et al. (2009) where a Overall, numerous studies have shown the abilities of SPI as
change of wall/core ratio from 1/1 to 1/3 involved a decrease of MEE an encapsulating agent, using both spray-drying and coacervation
from 92% to 79%. Jun-xia et al. (2011) attributed this tendency to techniques. In both methods, specific parameters affect microen-
incomplete emulsification after addition of excessive oil in system. capsulation efficiency and microparticle size, particularly the active
Unemulsified oil affected the electrostatic interactions between soy core concentration (Lazko et al., 2004a; Mendanha et al., 2009; Rusli
proteins and gum Arabic, and thus emulsion destabilization. et al., 2006; Yu et al., 2007), but authors showed that high values of
The protein concentration (as wall material) during the emul- MEE could be attained in both cases, by using suitable experimental
sification step is strongly related to the stability and size of conditions. The main differences between these two methods are
coacervates. This could be explained by the specific surface of oil the structure of the microparticles obtained, and consequently the
droplets, which is inversely proportional to their mean diameter release of the active core, and the microparticle sizes, usually higher
in emulsion (Lazko et al., 2004a). Due to protein surfactant proper- with coacervation (less than 100 ␮m for spray dried microparticles
ties, increasing protein concentration would result in an increase instead of generally more than 100 ␮m for coacervated microcap-
in oil droplet specific surface, improving the adsorption of proteins sules).
on the oil–water interface and the droplets’ coalescence resistance,
and thus a decrease in their mean diameter (generally detected 3.2. Pea proteins
by light scattering). On the other hand, Lazko et al. (2004a) also
demonstrated that protein concentration does not seem to have a Pea proteins are extracted from pea seeds where they repre-
significant influence on the microcapsule wall thickness. sent a 20% to 30% fraction including mainly globulins (65–80%) and
Some authors (Lazko et al., 2004a) have noticed that microen- two minority fractions, albumins and glutelins. Globulins comprise
capsulation by the coacervation method is more effective under three different proteins – legumin, vicilin and convicilin (Koyoro
acidic pH and high temperature conditions (pH 2 and 55 ◦ C, and Powers, 1987). Pea legumin represents the 11S globulin frac-
respectively). Acid mediums favor 11S globular protein denaturation with a molar mass between 350 and 400 kDa, while vicilin and
tion, characterized by deformation of their quaternary structure convicilin represent the 7S globulin fraction with a molar mass of
to secondary and tertiary structures. The overall accessibility of about 150 kDa.
hydrophobic protein sites inside the spherical formations can be Pea proteins extracted from grains possess interesting gel-
improved by this structure change (Magdassi, 1996; Wagner and forming (Akintayo et al., 1999) and emulsifying (Raymundo et al.,
Gueguen, 1995). At pH’s below the isoelectric point, the protein 2005) properties. However, in the literature for microencapsulation
COO− functions become uncharged COOH groups, and protein uses, these proteins are generally associated with polysaccharides
hydrophilicity decreases. Thus, an acidic medium would favor the (Ducel et al., 2004b; Gharsallaoui et al., 2010; Pereira et al., 2009;
affinity between proteins and the hydrophobic active core in the Pierucci et al., 2006, 2007). Indeed, polysaccharide/protein inter-
emulsions, which should result in improved MEE. actions give new functions to pea proteins without chemical or
When microencapsulation is undertaken by coacervation, a enzymatic modification, particularly solubility, foaming and surfac-
cross-linking step is often added at the end of the process, mainly tant properties (Liu et al., 2010). These interactions can also create
to reinforce the microcapsule shells. This supplementary step stable emulsions and thus give better particle size distribution and
would not affect the efficiency of protein precipitation around oil improve the efficiency of the microencapsulation process. Table 3
droplets, but would play an important role in emulsion stability, shows various pea protein/polysaccharide pairs and the different
and consequently on microcapsule size and dispersion, particularly processes used for active core microencapsulation.
with prolonged stirring. Without reticulation, the coalescence of
microcapsules was observed, resulting in a significant increase in 3.2.1. Microencapsulation by spray-drying
microcapsule average diameter (from 90 ␮m to more than 200 ␮m), Several studies deal with pea proteins as wall material for
whereas this coalescence is absent when microcapsules were microencapsulation, using the spray-drying technique. The main
cross-linked (no change in microcapsule diameter was observed) properties of the microparticles obtained are summarized in
(Lazko et al., 2004a). Glutaraldehyde is the most commonly used Table 4. Utilization of protein/polysaccharide mixtures allows
cross-linking agent, allowing stable microcapsule dispersion to be the possibility of combining the specific properties of each of
obtained over time (Lazko et al., 2004b), plus better mechanical these polymers. Polysaccharide products possess low emulsifica-
properties. But glutaraldehyde is a relatively toxic product, which tion properties compared to proteins, and are usually used as
limits its use in applications such as the food industry (Leung, 2001). wall materials in the presence of a surface-active constituent.
Table 3
Microencapsulation based on the complexes pea protein/polysaccharide as a wall material.
Protein Polysaccharide
Complex coacervation Pea globulins Gum Arabic, carboxy-methylcellulose, Triglyceride Ducel et al. (2004a,b)
sodium alginate
Spray-drying Pea proteins Maltodextrin Ascorbic acid Pierucci et al. (2006)
Spray-drying Pea proteins Maltodextrin ␣-Tocopherol Pierucci et al. (2007)
Spray-drying Pea proteins Maltodextrin Ascorbic acid Pereira et al. (2009)
Spray-drying Pea proteins (as additive) Pectin, maltodextrin Triglyceride Gharsallaoui et al. (2010)
The incorporation of carbohydrates with proteins as the encap- two coacervation processes were not made under exactly the same
sulated matrix, gives increased emulsion stability and better conditions, for example temperatures of 30 ◦ C and 55 ◦ C, pH values
protection of active ingredients against oxidation (Young et al., of 3.5 and 2.0, mechanical stirring at 500 rpm and magnetic stirring
1993). Gharsallaoui et al. (2010) noted that in protein/carbohydrate at 600 rpm, for pea proteins and soy proteins, respectively.
blends, proteins serve as an emulsifying and film-forming agent, It is apparently also possible to prepare microparticles from one
while polysaccharides act as a matrix forming material. The fraction of pea proteins (legumin: Irache et al., 1995 or vicilin:
retention of the active core observed in pea protein micropar- Ezpeleta et al., 1996a, 1997) without polysaccharide addition, and
ticles is similar to (or better than) in the particles with a to coat an active material, and these studies involved microparticle
protein/carbohydrate mixture. This, presumably, is induced by preparation (with legumin or vicilin) using simple coacervation.
electrostatic interactions between proteins and encapsulated Concerning particle size distribution, the mean particle diameter
material (Pierucci et al., 2007). As stated in the literature, the addi- varied from 200 to 700 nm. Finally, the average sizes of microcap-
tion of maltodextrin to the pea protein wall material increases sules based on pea proteins obtained by coacervation, varied from
the particle size, in particular for a hydrosoluble active material about 10, to hundreds of microns, while for spray-dried micro-
(Pierucci et al., 2006). The authors justified this increase by the fact spheres, the average size is always less than or near 10 ␮m.
that maltodextrin can induce the rapid formation of a glassy sur-
face which would allow air expansion inside microparticles, giving 3.2.3. Pea proteins as an additive for microencapsulating systems
an increase in particle diameter. The emulsifying properties of pea proteins (Ducel et al., 2004a)
The results reported, demonstrate that pea proteins alone or make them potentially useful as an additive to improve emul-
in association with polysaccharides are totally appropriate for the sion stabilization instead of as a simple main wall material.
microencapsulation of hydrophilic (ascorbic acid: Pereira et al., Gharsallaoui et al. (2010) used a small amount of pea protein
2009; Pierucci et al., 2006) hydrophobic (␣-tocopherol: Pierucci (0.5%, w/w) as an emulsifier to form oil-in-water emulsion contain-
et al., 2007; and triglyceride: Ducel et al., 2004b; Gharsallaoui et al., ing small oil droplets. Then pectin and maltodextrin were added,
2010) active core materials. to produce an emulsion containing triglyceride droplets coated
with protein–polysaccharide membranes. This study confirmed the
3.2.2. Microencapsulation by coacervation interest of combining the properties of polysaccharides with those
Ducel et al. (2004a,b) examined the use of pea globulin (isoelec- of proteins. The emulsions with polysaccharides seemed to be less
tric point in a pH range 4.4–4.6) for triglyceride microencapsulation sensitive to pH variations, high ionic strengths and high tempera-
by complex coacervation (Table 3), plus the influence of pH and tures, than those with only proteins (Dickinson, 2003; McClements,
polymer concentration on the microcapsule size. Increasing pea 1999). In addition, the hydrophobic polypeptides of proteins, added
globulin/gum Arabic (50:50) blend concentration in the initial to polysaccharide based emulsions, have a high capacity to adsorb
makeup, resulted in increased microcapsule size. For example, at at the oil–water interfaces, (for example pea globulin at acid pH)
pH 3.5, microcapsule diameters varied from 28 ␮m to 97 ␮m with and thus to stabilize emulsions (Gharsallaoui et al., 2010). These
a concentration change of 1 g/L to 10 g/L, respectively. Conversely, studies show that the use of small quantities of protein could stabi-
Lazko et al. (2004a) observed a decrease of coacervate size with lize emulsions against coalescence, pH and temperature variations.
an increase of soy protein concentration. In fact, the mean diam- To sum up, pea extracted proteins show convenient encapsu-
eter of microparticles obtained, decreased from 153 ␮m to 88 ␮m lating properties and are used for active material protection or
as the protein concentration increased from 0.5 g/L to 5 g/L, respec- for emulsion stabilization. Properties of the resulting microparti-
tively. This discordance between published results was probably cles were dependent on the microencapsulation technique used,
due to coacervation process differences. Complex coacervation was process conditions and the use of additives such as polysaccharides.
used in the case of pea proteins, and particle agglomeration and
coalescence increased their size. The presence of polysaccharides 3.3. Wheat proteins and other cereal proteins
in the initial preparation can also influence coacervate agglomer-
ation (Klassen and Nickerson, 2012). On the other hand, simple Wheat contains a specific protein: gluten, obtained as a by-
coacervation was used for preparing soy protein microparticles. product during starch isolation from wheat flour. The latter is a
Higher concentrations of surface active protein in the emulsion complex material, composed of proteins and a small polysaccharide
increased the coalescence resistant coacervates. In addition, the fraction. Its two main components are gliadin and glutenin. Gliadin
Table 4
The properties of microparticles produced by spray-drying with the pea proteins as a wall material (wall/core ratio of 2/1, w/w).
Wall material Core material Microparticle size (␮m) MEE (%) Core amount (g/100 g powder) Reference
Pea proteins ␣-Tocopherol 2.2 86.8 28 Pierucci et al. (2007)

Pea proteins/maltodextrin (1/1, w/w) ␣-Tocopherol 3.5 77.8 25
Pea proteins Ascorbic acid 2.7 101.9 34.6 Pierucci et al. (2006)
Pea proteins/maltodextrin (1/1, w/w) Ascorbic acid 8.2 95.9 29
is composed of single chain polypeptides, with an average molecu- structure with diameters ranging from 1 to 5 ␮m. These proteins
lar weight of 25–100 kDa, linked by intramolecular disulfide bonds, had a good capacity for protecting fish oil against oxidation in food
and soluble in neutral 70% ethanol. Glutenin is a hydrosoluble frac- preparations.
tion consisting of gliadin-like subunits stabilized by intermolecular Andreani et al. (2009) worked on wheat gluten microspheres
disulfide bonds in large aggregates, with a molecular weight greater for the controlled release of a model drug (diltiazem), and eval-
than 105 kDa (Bietz and Rothfus, 1970). uated the effect of a small amount of poly(ethylene oxide) on
Gluten represents approximately 80% of wheat seed proteins, microsphere properties. They demonstrated that perfectly spher-
plays an important role in wheat flour quality (Day et al., 2006), ical porous microspheres could be obtained, with mean particle
and is used essentially as a human and animal food source. While diameters of between 10 and 20 ␮m, and encapsulation efficiency
its insoluble nature is an important property for traditional appli- from 73% to 97%. They showed that the addition of 5% (w/w) of
cations, particularly in bread and baked products, this insolubility PEO to the gluten matrix improved the MEE significantly. This is
in water limits its use in many other applications such as cosmetics probably due to higher porosity of microparticles with PEO, and
and drugs. therefore greater specific surface area favoring better incorpora-
Wheat gluten is the cereal protein most studied in the microen- tion of the active core material. The effect of nature of solvent
capsulation field (Ducel et al., 2004b, 2005; Ezpeleta et al., 1996b; was studied by Ezpeleta et al. (1996b). They observed significant
Iwami et al., 1987; Mauguet et al., 2002; Yu and Lee, 1997). Its low variations in microparticle diameter, according to solvent compo-
water solubility and its viscoelasticity provide this plant polymer sition, highlighting the influence of physico-chemical interactions
with various interesting physico-chemical characteristics, such as between proteins and solvents. Antimicrobial chicken egg white
gel- and film-forming properties (Sun et al., 2009). Wheat pro- lysozyme, was encapsulated by zein protein using a supercriti-
teins alone, or in combination with polysaccharides are good for cal anti-solvent process (Zhong et al., 2009), and heterogeneously
encapsulating active core materials using various techniques. Some sized microparticles, ranging from a few to 50 ␮m and 46.5% MEE
studies have also been made with other cereal proteins as a wall were obtained. The active material release kinetics showed very
material: barley protein or corn zein (Parris et al., 2005; Wang promising microparticle properties for use in food production.
et al., 2011a,b; Zhong et al., 2009; Patel et al., 2012). Barley pro- In short, cereal proteins are relevant biomaterials as a matrix for
teins, studied by Wang et al. (2011b), are composed of two protein microencapsulation. They perform well for microencapsulation of
fractions: glutelin and hordein. Both these fractions show excel- hydrophobic and hydrophilic compounds alone, as well as mixed
lent film-forming and emulsifying properties (Wang et al., 2011a). with polysaccharides or synthetic polymers.
Corn extracted prolamin – zein is a protein fraction soluble in
hydro-alcoholic solutions and well-known for its good filmogenic 3.4. Other vegetable proteins potentially useful in
properties (Beck et al., 1996). Table 5 summarizes microencapsu- microencapsulation
lation studies with these biopolymers.
Other proteins have properties making them possible con-
3.3.1. Microencapsulation by coacervation tenders as wall material in microencapsulation, and this is
Ducel et al. (2005) studied the encapsulation of vaseline oil with especially true for rice proteins, oat proteins and sunflower
a gliadin/gum Arabic wall, by complex coacervation, focusing on proteins. Rice and oat proteins already have a large range of applica-
protein concentration and effect of pH on microcapsule proper- tions in the food sector. However, the physico-chemical properties
ties. They found that a decrease in medium pH (from 3.5 to 3) gave of sunflower proteins have been extensively studied, and this natu-
an increase in viscoelasticity and a decrease in microcapsule aver- ral polymer has no major industrial uses, meaning that it would be
age size (from 50 ␮m to 25 ␮m). The wall polymer distribution on interesting to find new applications and develop high added-value
the droplet surface was more homogeneous so particle aggrega- products based on them.
tion was reduced. Encapsulation conditions and efficiency were
improved by the pH decrease. Analogous behavior for a pea pro- 3.4.1. Rice proteins
tein/gum Arabic encapsulating system, has been observed (Ducel Rice is among the most important cereal crops in the world.
et al., 2004a,b), and this result agrees with observations by Lazko It is established as the basic foodstuff for over half the world’s
et al. (2004a) concerning complex coacervation microencapsula- population. Containing from 12 to 20% proteins, rice bran, mainly
tion using soy glycinin. The range of wheat protein microcapsule removed from the grain during the milling process to produce white
size using coacervation (simple or complex) can vary from a few to rice, may be a potential source of inexpensive high quality pro-
two hundred micrometers (Ducel et al., 2005; Mauguet et al., 2002; teins (Hamada, 2000). Compared to rice bran, the protein content
Yu and Lee, 1997). These values are in line with those obtained from in rice grains is slightly lower, varying from 6 to 15% (Bienvenido,
pea protein and soy protein microcapsules (Ducel et al., 2004b; 1994). Rice proteins are generaly prepared by alkali extraction fol-
Lazko et al., 2004a). lowed by isoelectric precipitation (Kaewka et al., 2009; Pinciroli
et al., 2009) and by subcritical water treatement (Hata et al., 2008;
3.3.2. Microencapsulation using other processes Sereewatthanawut et al., 2008). In addition, rice has also been stud-
Only a few studies deal with wheat proteins for spray drying ied for the production of starch, monosodium glutamate, pigments
microencapsulation. Iwami et al. (1987) reported the encapsula- and rice wine; thus rice protein could be an additional by-product
tion of linoleic acid in a gliadin matrix to improve its stability to be exploited (Cao et al., 2009). After the sequential extraction of
and digestibility, particularly for bread making applications. Wheat rice protein fractions, the following distribution has been obtained:
proteins were also used as wall material for microencapsula- about 75% glutenin, 15% globulin, 6% albumin and 3% prolamin
tion with the solvent evaporation method (Andreani et al., 2009; (Agboola et al., 2005).
Ezpeleta et al., 1996b), and proteins extracted from barley seeds Chandi and Sogi (2007) analyzed the functional properties of rice
were used as carrier material for fish oil microencapsulation by protein concentrate (55% of the protein fraction). They noticed the
Wang et al. (2011a,b). The spray-drying method was used for excellent foaming stability lasting several days, the high emulsify-
microparticle preparation with an inlet temperature of 150 ◦ C. ing capacity in sugar based (5–15%, w/w) solutions, and the good
The authors demonstrated 97–100% encapsulation efficiency and stability of emulsions depending on the pH and salt/sugar pres-
high oil content in the powder – around 50%. The barley protein ence. The physico-chemical properties are similar to those of casein
microparticles obtained have a spherical shape and porous inner (Chandi and Sogi, 2007).
Table 5
Cereal proteins in the microencapsulation.
Spray-drying Wheat gliadin, corn zeine Linoleic acid Iwami et al. (1987)
Spray-drying Barley protein Fish oil Wang et al. (2011a,b)
Simple coacervation Gluten/casein Pyrrolnitrin Yu and Lee (1997)
Simple coacervation Gliadin Hexadecane Mauguet et al. (2002)
Complex coacervation ␣-Gliadin/Arabic gum Vaselin oil Ducel et al. (2004a,b, 2005)
Solvent evaporation Gliadin Retinoic acid Ezpeleta et al. (1996a,b)
Solvent evaporation Gluten/poly(ethylen oxide) Diltiazem hydrochloride Andreani et al. (2009)
Phase separation Corn zein Essential oils Parris et al. (2005)
Supercritical anti-solvent process Corn zein Lysozyme Zhong et al. (2009)
Anti-solvent precipitation method Corn zein Quercetin Patel et al. (2012)
Rice bran isolate containing approximately 92% protein is pre- 17–23% of total proteins and two minor fractions glutelins and
pared from defatted rice bran and its properties have been studied prolamins give 11–17% and 1–4% protein fractions, respectively.
(Wang et al., 1999). They showed that: the foaming properties of In terms of sedimentation coefficients, sunflower proteins show
rice protein are similar to those of albumin from egg white; the two major fractions: the 11S globulins (also named helianthinin)
emulsifying capacities of albumin from bovine serum (BSA) are and the 2S albumins. Helianthinin has been reported to be
significantly higher than those of rice proteins; minimum protein present as a globular oligomeric protein with a molecular weight
solubility is close to the isoelectric point at pH 4 and the maximum of 300–350 kDa (Gonzalez-Perez and Vereijken, 2007), and this
at pH 10; the main amino acid content of rice proteins is similar protein mainly exists in the 11S form (hexametric structure).
to that of casein and soy proteins; the denaturation temperature of Depending on pH, ionic strength, temperature and protein concen-
rice protein isolate is about 83.4 ◦ C. tration, helianthinin may also occur in the 15–18S, 7S or 3S forms.
Rice proteins also associate well with polysaccharides (alginate In 11S sunflower proteins, different subunits are traditionally pro-
and carrageenan) to form complex precipitates with possible new cessed to give an acidic and a basic polypeptide linked by a single
industrial applications (Fabian et al., 2010). From these results, disulfide bond. These basic and acidic polypeptides range in molec-
the physico-chemical properties of rice proteins could provide ular weight from about 21 to 27 kDa and from about 32 to 44 kDa,
favorable characteristics for wall material in microencapsulation. respectively. The solubility of helianthinin with a minimum of 4–5.5
However overall, rice protein use concerns the food industry, depends strongly on pH and ionic strength.
rather than potential low volume, high added value applications Albumin proteins from sunflower, with a sedimentation coef-
of microencapsulation. ficient of approximately 2S and molecular weights ranging from
10 to 18 kDa, show good solubility in aqueous solutions, indepen-
3.4.2. Oat proteins dent of pH and ionic strength. Contrary to the majority fractions,
Oats is one of the most popular cereals for human and animal the functional properties of glutelins and prolamins from sunflower
foods because of its high protein and fatty acid content. Protein seeds have not been reported in the literature.
content in oat grain is one of the highest, varying from 12 to 24% The amino acid composition of soy proteins (Kovalenko et al.,
(Chronakis et al., 2004). The average amino acid composition of oat 2006) and sunflower proteins (Conde et al., 2005) are shown in
proteins is very attractive from a nutritional value point of view, and Fig. 3. Some similarities in total amino acid content for these
this is probably related to the higher proportion of albumins and vegetable proteins can be seen. The physico-chemical properties
globulins compared to proteins from the other cereal grains. Glob- of sunflower proteins have already been studied (Gonzalez-Perez
ulin represents the major part of oat proteins (around 70–80%). Oat et al., 2005; Molina et al., 2004; Patino et al., 2007). Most authors
protein concentrate has poor solubility and functional properties. showed that sunflower preparations have better (or at least sim-
To improve these physico-chemical properties, modifications such ilar) emulsifying properties as those of soy protein preparations.
as enzymatic hydrolysis (Yao et al., 2007), acetylation and succiny- The main results of these studies showed that the highest emulsi-
lation (Mohamed et al., 2009) were carried out, and demonstrated fying capacity is observed in the pH range of 7–8 and the minimum
that these chemical modifications could improve the solubility, at the isoelectric pH of 4.3; the extraction method and solvent used
emulsifying activity and foaming capacity of oat proteins. for protein extraction does not change the emulsifying ability of
In conclusion, oat native proteins do not offer the required proteins; heating involving protein denaturation, increases the sta-
properties to be used in microencapsulation, but some specific bility of emulsions but reduces their emulsifying capacities. This
modifications could allow them to be considered as wall materials. latter observation can be explained by the change of protein struc-
ture during heating denaturation, favoring chain unfolding and
3.4.3. Sunflower proteins increased conformational flexibility. Thus the surface-active capac-
Sunflowers are mainly cultivated for the production of oil ity of unfolded sunflower proteins becomes lower during emulsion
extracted from their seeds, and they are one of the major sources formation, but after emulsion preparation it stays stable longer.
of edible oil. Proteins are the majority constituents in sunflower Concerning foam properties, sunflower proteins seemed to
oil cakes, valued essentially as animal feed. The defatted sunflower be less efficient at forming foam than soy proteins. Neverthe-
flour contains a high quantity of proteins, around 27% in dry weight less, sunflower protein foams are stable over time at a basic
(Ordonez et al., 2001). The dehulled seed consists of about 20–40% pH and a high concentration. Chemical modifications (for exam-
crude protein, this value being highly affected by sunflower vari- ple enzymatic hydrolysis) of sunflower proteins could lead to an
ety (Gonzalez-Perez and Vereijken, 2007). The quantity of proteins improvement in their functional properties and to new interesting
extracted from the sunflower, also varies according to used solvent applications (Conde and Patino, 2007). The presence of phenolic
(mainly aqueous solutions) and the extraction conditions (stirring compounds in sunflower proteins, which cause the green-brown
mode, temperature, pH). In the sunflower oil cake, four fractions color of its powder, limits their development as a source of food
of proteins are present (Linden, 1994): globulins constitute the proteins for humans. Therefore, there could be very interesting
main fraction ranging from 55 to 60%; albumins account for about new openings for these proteins in non-food industrial sectors.
Fig. 3. Amino acid composition of soy (Kovalenko et al., 2006) and sunflower (Conde et al., 2005) proteins, every amino acid fraction is presented in g/100 g of protein isolate.
Microencapsulation could be one possibility for an industrial appli- encapsulation technique, use of additives or proteins combined
cation of this agricultural by-product. with polysaccharides.
Other inexpensive proteins extracted from rice, oat or sunflower
4. Industrial applications of microencapsulation by seeds are known for their interesting functional properties and
vegetable proteins could be suitable microencapsulation wall forming materials. These
natural polymers show good solubility, emulsion forming ability
Pea proteins show a good properties for their potential appli- and foaming stability, giving them the appropriate characteristics
cation, in particular for the production of adhesives, bioplastics, for potential use as efficient coating materials. Moreover, they can
emulsifiers and wall forming materials for microencapsulation (De be associated with polysaccharides as is commonly the case in
Graaf et al., 2001). However, these proteins are no suggested to be microencapsulation. Thus, the good physico-chemical properties
used in technical applications. The functional properties of wheat of all these vegetable proteins open a new path for specific appli-
proteins and corn zein also suggest several potential applications cations, the development of innovative delivery systems, and/or
for these natural polymers in the fields of adhesives, matrix mate- functional food products.
rials for microencapsulation, textiles, cosmetics and biodegradable Some limitations of vegetable protein use for making high added
plastics (Shukla and Cheryan, 2001). For both of these proteins, value products could be the extraction cost to obtain high-quality
there is still no actual industrial application in microencapsulation, proteins, low solubility of some proteins and large polydispersity in
but they are potentially good candidates. the size of naturally occurring protein chains. Compared to other
Conversely, soy bean proteins are already used as wall forming bio based materials for microencapsulation, such as polysaccha-
materials in the food industry, in particular to mask the undesir- rides, synthetic polymers or animal-based proteins, plant extracted
able taste of some nutritional additives (bioactive compounds for vegetable proteins represent a very promising source of polymers
athletes, such as casein hydrolysate) (Favaro-Trindade et al., 2010; with interesting functional properties. Their use as a wall material
Mendanha et al., 2009; Ortiz et al., 2009; Sun-Waterhouse and augurs well for the encapsulation of hydrophilic and hydrophobic
Wadhwa, 2012) or to protect components sensitive to oxidation substances by different techniques, and production of microparti-
and\or volatile aromas (orange oil) (Gharsallaoui et al., 2007; Kim cles, with good microencapsulation efficiency and various potential
et al., 1996; Xiao et al., 2011). applications.
5. Conclusions and future prospects References
The use of vegetable proteins as a wall material for microencap- Agboola, S., Ng, D., Mills, D., 2005. Characterisation and functional properties of
sulation of various sensitive materials, reflects the actual “green” Australian rice protein isolates. J. Cereal Sci. 41, 283–290.
Akintayo, E.T., Oshodi, A.A., Esuoso, K.O., 1999. Effects of NaCl, ionic strength and pH
tendency in the food, pharmaceutical and cosmetics industries. on the foaming and gelation of pigeon pea (Cajanus cajan) protein concentrates.
The two main techniques used for microencapsulation of different Food Chem. 66, 51–56.
core substances by these natural polymers, are spray-drying and Andreani, L., Cercena, R., Ramos, B.G.Z., Soldi, V., 2009. Development and charac-
terization of wheat gluten microspheres for use in a controlled release system.
coacervation. Particle morphology is very dependent on the pro- Mater. Sci. Eng. 29, 524–531.
cess chosen, mainly because coacervation produces microcapsules, Augustin, M.A., Sanguansri, L., Bode, O., 2006. Maillard reaction products as encap-
whereas microspheres are generally obtained with spray-drying. sulants for fish oil powders. J. Food Sci. 71, 25–32.
Bayomi, M.A., Al-Suwayeh, S.A., El-Helw, A.M., Mesnad, A.F., 1998. Preparation of
Vegetable proteins widely used as encapsulants are pea protein casein–chitosan microspheres containing diltiazem hydrochloride by an aque-
isolate, soy protein isolate, wheat gliadins, corn zein and barley ous coacervation technique. Pharm. Acta Helv. 73, 187–192.
protein. The various studies have proved the ability of proteins to Beck, M., Tomka, I., Waysek, E., 1996. Physico-chemical characterization of zein as
a film polymer. A direct comparison with ethyl cellulose. Int. J. Pharm. 141,
efficiently protect different forms of active materials (hydrophilic
137–150.
or hydrophobic, solid or liquid) as an encapsulating agent, using Benita, S., 2006. Microencapsulation. Methods and Industrial Applications, 2nd ed.
both spray-drying and coacervation methods. However, microen- Taylor and Francis Group, New York/London.
capsulation efficiency, preparation stability and microparticle size Bienvenido, O.J., 1994. Le riz dans la nutrition humaine. Organisation des nations
unies pour l’alimentation et l’agriculture, Rome.
could be affected by different parameters, such as active core Bietz, J.A., Rothfus, J.A., 1970. Comparison of peptides from wheat gliadin and
and wall material concentrations, temperature and pH of media, glutenin. Cereal Chem. 47, 381–392.
Cao, X., Wen, H., Li, C., Gu, Z., 2009. Differences in functional properties and bio- Hamada, J.S., 2000. Characterization and functional properties of rice bran pro-
chemical characteristics of congenetic rice proteins. J. Cereal Sci. 50, 184–189. teins modified by commercial exoproteases and endoproteases. J. Food Sci. 65,
Chandi, G.K., Sogi, D.S., 2007. Functional properties of rice bran protein concentrates. 305–310.
J. Food Eng. 79, 592–597. Hata, S., Wiboonsirikul, J., Maeda, A., Kimura, Y., Adachi, S., 2008. Extraction
Charve, J., Reineccius, G.A., 2009. Encapsulation performance of proteins and tradi- of defatted rice bran by subcritical water treatment. Biochem. Eng. J. 40,
tional materials for spray dried flavors. J. Agric. Food Chem. 57, 2486–2492. 44–53.
Chen, L., Subirade, M., 2009. Elaboration and characterization of soy/zein pro- Higuera-Ciapara, I., Felix-Valenzuela, L., Goycoolea, F.M., Arguelles-Monal, W., 2004.
tein microspheres for controlled nutraceutical delivery. Biomacromolecules 10, Microencapsulation of astaxanthin in a chitosan matrix. Carbohydr. Polym. 56,
3327–3334. 41–45.
Choi, Y.S., Choi, J.H., Han, D.J., Kim, H.Y., Lee, M.A., Jeong, J.Y., Chung, H.J., Kim, C.J., Huang, S.B., Wu, M.H., Lee, G.B., 2010. Microfluidic device utilizing pneumatic micro-
2010. Effects of replacing pork back fat with vegetable oils and rice bran fiber vibrators to generate alginate microbeads for microencapsulation of cells. Sens.
on the quality of reduced-fat frankfurters. Meat Sci. 84, 557–563. Actuat. 147, 755–764.
Chronakis, I.S., Fredholm, A., Triantafyllou, A.O., Oste, R., 2004. Complex formation Irache, J.M., Bergougnoux, L., Ezpeleta, I., Gueguen, J., Orecchioni, A.M., 1995.
in aqueous medium of partially hydrolysed oat cereal proteins with sodium Optimization and in vitro stability of legumin nanoparticles obtained by a coac-
stearoyl-2 lactylate (SSL) lipid surfactant and implications for bile acids activity. ervation method. Int. J. Pharm. 126, 103–109.
Colloid Surf. 35, 175–184. Iwami, K., Hattori, M., Nakatani, S., Ibuki, F., 1987. Spray-dried gliadin powders
Conde, J.M., Escobar, M.M., Pedroche, J.J.J., Rodríguez, F.M., Rodriguez, P.J.M., 2005. inclusive of linoleic acid (microcapsules): their preservability, digestibility and
Effect of enzymatic treatment of extracted sunflower proteins on solubil- application to bread making. Agric. Biol. Chem. 51, 3301–3307.
ity, amino acid composition, and surface activity. J. Agric. Food Chem. 53, Jenkins, J.A., Breiteneder, H., Mills, E.N., 2007. Evolutionary distance from human
8038–8045. homologs reflects allergenicity of animal food proteins. J. Allergy Clin. Immunol.
Conde, J.M., Patino, J.M.R., 2007. The effect of enzymatic treatment of a sunflower 120, 1399–1405.
protein isolate on the rate of adsorption at the air–water interface. J. Food Eng. Jeon, Y.J., Vasanthan, T., Temelli, F., Song, B.K., 2003. The suitability of barley and
78, 1001–1009. corn starches in their native and chemically modified forms for volatile meat
Day, L., Augustin, M.A., Batey, I.L., Wrigley, C.W., 2006. Wheat-gluten uses and indus- flavor encapsulation. Food Res. Int. 36, 349–355.
try needs. Trends Food Sci. Technol. 17, 82–90. Jiménez-Yan, L., Brito, A., Cuzon, G., Gaxiola, G., García, T., Taboada, G., Soto, L.A.,
De Graaf, L.A., Harmsen, P.F.H., Vereijken, J.M., Monikes, M., 2001. Requirements for Brito, R., 2006. Energy balance of Litopenaeus vannamei postlarvae fed on animal
non-food applications of pea proteins. A review. Nahrung/Food 45, 408–411. or vegetable protein based compounded feeds. Aquaculture 260, 337–345.
Dickinson, E., 1999. Adsorbed protein layers at fluid interfaces: interactions, struc- Jun-xia, X., Hai-yan, Y., Jian, Y., 2011. Microencapsulation of sweet orange oil by
ture and surface rheology. Colloid Surf. 15, 161–176. complex coacervation with soybean protein isolate/gum Arabic. Food Chem.
Dickinson, E., 2001. Milk protein interfacial layers and the relationship to emulsion 125, 1267–1272.
stability and rheology. Colloid Surf. 20, 197–210. Jyothi, N.V.N., Prasanna, P.M., Sakarkar, S.N., Prabha, K.S., Ramaiah, P.S., Srawan,
Dickinson, E., 2003. Hydrocolloids at interfaces and the influence of the properties G.Y., 2010. Microencapsulation techniques, factors influencing encapsulation
of dispersed system. Food Hydrocolloid 17, 25–39. efficiency. J. Microencapsul. 27, 187–197.
Drusch, S., 2007. Sugar beet pectin: a novel emulsifying wall component for microen- Kaewka, K., Therakulkait, C., Cadwallader, K.R., 2009. Effect of preparation conditions
capsulation of lipophilic food ingredients by spray-drying. Food Hydrocolloid 21, on composition and sensory aroma characteristics of acid hydrolyzed rice bran
1223–1228. protein concentrate. J. Cereal Sci. 50, 56–60.
Dubey, R., Shami, T.C., Bhasker Rao, K.U., 2009. Microencapsulation technology and Kim, Y.D., Morr, C.V., Schenz, T.W., 1996. Microencapsulation properties of gum Ara-
application. Defence Sci. J. 59, 82–95. bic and several food proteins: spray-dried orange oil emulsion particles. J. Agric.
Ducel, V., Richard, J., Popineau, Y., Boury, F., 2004a. Adsorption kinetics and rhe- Food Chem. 44, 1314–1320.
ological interfacial properties of plant proteins at the oil–water interface. Klassen, D.R., Nickerson, M.T., 2012. Effect of pH on the formation of electrostatic
Biomacromolecules 5, 2088–2093. complexes within admixtures of partially purified pea proteins (legumin and
Ducel, V., Richard, J., Popineau, Y., Boury, F., 2005. Rheological interfacial properties vicilin) and gum Arabic polysaccharides. Food Res. Int. 46, 167–176.
of plant protein-Arabic gum coacervates at the oil–water interface. Biomacro- Kovalenko, I.V., Rippke, G.R., Hurburgh, C.R., 2006. Determination of amino acid com-
molecules 6, 790–796. position of soybeans (Glycine max) by near-infrared spectroscopy. J. Agric. Food
Ducel, V., Richard, J., Saulnier, P., Popineau, Y., Boury, F., 2004b. Evidence Chem. 54, 3485–3491.
and characterization of complex coacervates containing plant proteins: Koyoro, H., Powers, J.R., 1987. Functional properties of pea globulin fractions. Cereal
application to the microencapsulation of oil droplets. Colloid Surf. 232, Chem. 64, 97–101.
239–247. Krishnan, S., Bhosale, R., Singhal, R.S., 2005. Microencapsulation of cardamom ole-
Eldem, T., Speiser, P., Hincal, A., 1991. Optimization of spray-dried and -congealed oresin: evaluation of blends of gum Arabic, maltodextrin and a modified starch
lipid micropellets and characterization of their surface morphology by scanning as wall materials. Carbohydr. Polym. 61, 95–102.
electron microscopy. Pharm. Res. 8, 47–54. Lazko, J., Popineau, Y., Legrand, J., 2004a. Soy glycinin microcapsules by simple
Ezpeleta, I., Irache, J.M., Stainmesse, S., Chabenat, C., Gueguen, J., Orecchioni, A.M., coacervation method. Colloid Surf. 37, 1–8.
1996a. Preparation of lectin–vicilin nanoparticle conjugates using the carbodi- Lazko, J., Popineau, Y., Renard, D., Legrand, J., 2004b. Microcapsules based on
imide coupling technique. Int. J. Pharm. 142, 227–233. glycinin-sodium dodecyl sulfate complex coacervation. J. Microencapsul. 21,
Ezpeleta, I., Irache, J.M., Stainmesse, S., Chabenat, C., Gueguen, J., Popineau, Y., 59–70.
Orecchioni, A.M., 1996b. Gliadin nanoparticles for the controlled release of all- Lee, K.E., Cho, S.H., Lee, H.B., Jeong, S.Y., Yuk, S.H., 2003. Microencapsula-
transretinoic acid. Int. J. Pharm. 131, 191–200. tion of lipid nanoparticles containing lipophilic drug. J. Microencapsul. 20,
Ezpeleta, I., Irache, J.M., Gueguen, J., Orecchioni, A.M., 1997. Properties of glu- 489–496.
taraldehyde cross-linkes vicilin nano- and microparticles. J. Microencapsul. 14, Leung, H.W., 2001. Ecotoxicology of glutaraldehyde: review of environmental fate
557–565. and effects studies. Ecotoxicol. Environ. Saf. 49, 26–39.
Fabian, C.B., Huynh, L.H., Ju, Y.H., 2010. Precipitation of rice bran protein using Li, H., Zhu, K., Zhou, H., Peng, W., 2012. Effects of high hydrostatic pressure treatment
carrageenan and alginate. Food Sci. Technol. 43, 375–379. on allergenicity and structural properties of soybean protein isolate for infant
Favaro-Trindade, C.S., Santana, A.S., Monterrey-Quintero,.E.S., Trindade, M.A., Netto, formula. Food Chem. 132, 808–814.
F.M., 2010. The use of spray drying technology to reduce bitter taste of casein Linden, G.L.D., 1994. Biochimie agro-industrielle: Valorisation alimentaire de la pro-
hydrolysate. Food Hydrocolloid 24, 336–340. duction agricole. Masson, Paris.
Franzen, K.L., Kinsella, J.E., 1976. Functional properties of succinylated and acety- Liu, S., Elmer, C., Low, N.H., Nickerson, M.T., 2010. Effect of pH on the functional
lated soy protein. J. Agric. Food Chem. 24, 788–795. behaviour of pea protein isolate-gum Arabic complexes. Food Res. Int. 43,
Gan, C.Y., Cheng, L.H., Easa, A.M., 2008. Evaluation of microbial transglutaminase 489–495.
and ribose cross-linked soy protein isolate-based microcapsules containing fish Magdassi, S., 1996. Surface Activity of Proteins Chemical and Physico-Chemical Mod-
oil. Innov. Food Sci. Emerg. Technol. 9, 563–569. ifications. Marcel Dekker, New York.
Gharsallaoui, A., Roudaut, G., Chambin, O., Voilley, A., Saurel, R., 2007. Applications Mauguet, M.C., Legrand, J., Brujes, L., Carnelle, G., Larre, C., Popineau, Y., 2002. Gliadin
of spray-drying in microencapsulation of food ingredients: an overview. Food matrices for microencapsulation processes by simple coacervation method. J.
Res. Int. 40, 1107–1121. Microencapsul. 19 (3), 377–384.
Gharsallaoui, A., Saurel, R., Chambin, O., Cases, E., Voilley, A., Cayot, P., 2010. Utili- McClements, D.J., 1999. Food Emulsions: Principles, Practice and Techniques. CRC
sation of pectin coating to enhance spray-dry stability of pea protein-stabilised Press, Boca Raton, FL.
oil-in-water emulsions. Food Chem. 122, 447–454. McClements, D.J., Decker, E.A., Weiss, J., 2007. Emulsion-based delivery systems for
Gonzalez-Perez, S., Vereijken, J.M., Koningsveld, G.A., Gruppen, H., Voragen, A., 2005. lipophilic bioactive components. J. Food Sci. 72, 109–124.
Physicochemical properties of 2S albumins and the corresponding protein iso- Mendanha, D.V., Ortiz, S.E.M., Favaro-Trindade, C.S., Mauri, A., Monterrey-Quintero,
late from sunflower (Helianthus annuus). J. Food Sci. 70, 98–103. E.S., Thomazini, M., 2009. Microencapsulation of casein hydrolysate by complex
Gonzalez-Perez, S., Vereijken, J.M., 2007. Sunflower proteins: overview of their coacervation with SPI/pectin. Food Res. Int. 42, 1099–1104.
physicochemical, structural and functional properties. J. Sci. Food Agric. 87, Merodio, M., Arnedo, A., Renedo, M.J., Irache, J.M., 2001. Ganciclovir-loaded albumin
2173–2191. nanoparticles: characterization and in vitro release properties. Eur. J. Pharm. Sci.
Gouin, S., 2004. Microencapsulation: industrial appraisal of existing technologies 12, 251–259.
and trends. Trends Food Sci. Technol. 15, 330–347. Mohamed, A., Biresaw, G., Xu, J., Hojilla-Evangelista, M., Rayas-Duarte, P., 2009. Oats
Gu, X., Campbell, L.J., Euston, S.R., 2009. Effects of different oils on the properties of protein isolate: thermal, rheological, surface and functional properties. Food Res.
soy protein isolate emulsions and gels. Food Res. Int. 42, 925–932. Int. 42, 107–114.
Molina, M.I., Petruccelli, S., Anon, M.S., 2004. Effect of pH and ionic strength modi- Ruiz-Henestrosa, V.P., Sanchez, C.C., Escobar, M.M.Y., Jimenez, J.J.P., Rodríguez, F.M.,
fications on thermal denaturation of the 11S globulin of sunflower (Helianthus Patino, J.M.R., 2007. Interfacial and foaming characteristics of soy globulins as a
annuus). J. Agric. Food Chem. 52, 6023–6029. function of pH and ionic strength. Colloid Surf. 309, 202–215.
Muller, R.H., Radtke, M., Wissing, S.A., 2002. Nanostructured lipid matrices for Rusli, J.K., Sanguansri, L., Augustin, M.A., 2006. Stabilization of oils by microencap-
improved microencapsulation of drugs. Int. J. Pharm. 242, 121–128. sulation with heated protein–glucose syrup mixtures. J. Am. Oil Chem. Soc. 83,
Munin, A., Edwards-Lévy, F., 2011. Encapsulation of natural polyphenolic com- 965–971.
pounds; a review. Pharmaceutics 3, 793–829. Saénz, C., Tapia, S., Chávez, J., Robert, P., 2009. Microencapsulation by spray drying of
Murúa-Pagola, B., Beristain-Guevara, C.I., Martínez-Bustos, F., 2009. Preparation of bioactive compounds from cactus pear (Opuntia ficus-indica). Food Chem. 114,
starch derivatives using reactive extrusion and evaluation of modified starches 616–622.
as shell materials for encapsulation of flavoring agents by spray drying. J. Food Sawashita, N., Naemura, A., Shimizu, M., Morimatsu, F., Ijiri, Y., Yamamoto, J., 2006.
Eng. 91, 380–386. Effect of dietary vegetable and animal proteins on atherothrombosis in mice.
Nesterenko, A., Alric, I., Silvestre, F., Durrieu, V., 2012. Influence of soy protein’s Nutrition 22, 661–667.
structural modifications on their microencapsulation properties: ␣-tocopherol Semyonov, D., Ramon, O., Kaplun, Z., Levin-Brener, L., Gurevich, N., Shimoni, E., 2010.
microparticles preparation. Food Res. Int. 48, 387–396. Microencapsulation of Lactobacillus paracasei by spray freeze drying. Food Res.
Nori, M.P., Favaro-Trindade, C.S., Alencar, S.M., Thomazini, S.M., Balieiro, J.C.C., 2010. Int. 43, 193–202.
Microencapsulation of propolis extract by complex coacervation. Food Sci. Tech- Sereewatthanawut, I., Prapintip, S., Watchiraruji, K., Goto, M., Sasaki, M., Shotipruk,
nol. 44, 429–435. A., 2008. Extraction of protein and amino acids from deoiled rice bran by sub-
Ordonez, C., Asenjo, M.G., Benitez, J.L., Gonzalez, J.L., 2001. Obtaining a protein con- critical water hydrolysis. Bioresour. Technol. 99, 555–561.
centrate from integral deffated sunflower flour. Bioresour. Technol. 78, 187–190. Shaikh, J., Bhosale, R., Singhal, R., 2006. Microencapsulation of black pepper oleo-
Ortiz, S.E.M., Mauri, A., Monterrey-Quintero, E.S., Trindade, M.A., 2009. Production resin. Food Chem. 94, 105–110.
and properties of casein hydrolysate microencapsulated by spray drying with Shukla, R., Cheryan, M., 2001. Zein: the industrial protein from corn. Ind. Crop. Prod.
soybean protein isolate. Food Sci. Technol. 42, 919–923. 13, 171–192.
Osborne, T.B., 1909. The Vegetable Proteins. Longmans, Green and Co., London. Sun-Waterhouse, D., Wadhwa, S.S., 2012. Industry-relevant approaches for minimis-
Parris, N., Cooke, P.H., Hicks, K.B., 2005. Encapsulation of essential oils in zein ing the bitterness of bioactive compounds in functional foods: a review. Food
nanospherical particles. J. Agric. Food Chem. 53, 4788–4792. Bioprocess Technol., http://dx.doi.org/10.1007/s11947-012-0829-2.
Patel, A.R., Heussen, P.C.M., Hazekamp, J., Dorst, E., Velikov, K.P., 2012. Quercetin Sun, S., Song, Y., Zheng, Q., 2009. Rheological behavior of heat-induced wheat gliadin
loaded biopolymeric colloidal particles prepared by simultaneous precipitation gel. Food Hydrocolloid 23, 1054–1056.
of quercetin with hydrophobic protein in aqueous medium. Food Chem. 133, Wagner, J.R., Gueguen, J., 1995. Effects of dissociation, deamidation, and reducing
423–429. treatment on structural and surface active properties of soy glycinin. J. Agric.
Patel, S.K., Lavasanifar, A., Choi, P., 2010. Molecular dynamics study of the encapsu- Food Chem. 43, 1993–2000.
lation capability of a PCL–PEO based block copolymer for hydrophobic drugs Wang, M., Hettiarachchy, N.S., Qi, M., Burks, W., Siebenmorgen, T., 1999. Preparation
with different spatial distributions of hydrogen bond donors and acceptors. and functional properties of rice bran protein isolate. J. Agric. Food Chem. 47,
Biomaterials 31, 1780–1786. 411–416.
Patino, J.M.R., Conde, J.M., Linaresa, H.M., Jimenez, J.J.P., Sanchez, C.C., Pizones, V., Wang, R., Tian, Z., Chen, L., 2011a. Nano-encapsulations liberated from barley pro-
Rodríguez, F.M., 2007. Interfacial and foaming properties of enzyme-induced tein microparticles for oral delivery of bioactive compounds. Int. J. Pharm. 406,
hydrolysis of sunflower protein isolate. Food Hydrocolloid 21, 782–793. 153–162.
Pedro, A.S., Cabral-Albuquerque, E., Ferreira, D., Sarmento, B., 2009. Chitosan: an Wang, R., Tian, Z., Chen, L., 2011b. A novel process for microencapsulation of fish oil
option for development of essential oil delivery systems for oral cavity care? with barley protein. Food Res. Int. 44, 2735–2741.
Carbohydr. Polym. 76, 501–508. Wikstrom, J., Elomaa, M., Syvajarvi, H., Kuokkanen, J., Yliperttula, M., Honkakoski, P.,
Pereira, H.V.R., Saraiva, K.P., Carvalho, L.M.J., Andrade, L.R., Pedrosa, C., Pierucci, Urtti, A., 2008. Alginate-based microencapsulation of retinal pigment epithelial
A.P.T.R., 2009. Legumes seeds protein isolates in the production of ascorbic acid cell line for cell therapy. Biomaterials 29, 869–876.
microparticles. Food Res. Int. 42, 115–121. Wilson, N., Shah, N.P., 2007. Microencapsulation of vitamins. ASEAN Food J. 14, 1–14.
Pierucci, A.P.T.R., Andrade, L.R., Baptista, E.B., Volpato, N.M., Rocha-Leao, M.H.M., Xiao, J.X., Yu, H.Y., Yang, J., 2011. Microencapsulation of sweet orange oil by com-
2006. New microencapsulation system for ascorbic acid using pea protein con- plex coacervation with soybean protein isolate/gum Arabic. Food Chem. 125,
centrate as coat protector. J. Microencapsul. 23, 654–662. 1267–1272.
Pierucci, A.P.T.R., Andrade, L.R., Farina, M., Pedrosa, C., Rocha-Leao, M.H.M., 2007. Yao, X.G.H., Chen, Z., Shan, L., Zhang, M., 2007. Some functional proper-
Comparison of a-tocopherol microparticles produced with different wall mate- ties of oat bran protein concentrate modified by trypsin. Food Chem. 10,
rials: pea protein a new interesting alternative. J. Microencapsul. 24, 201–213. 163–170.
Pinciroli, M., Vidal, A.A., Anon, M.C., Martínez, E.N., 2009. Comparison between pro- Yoo, S.H., Song, Y.B., Chang, P.S., Lee, H.G., 2006. Microencapsulation of ␣-tocopherol
tein functional properties of two rice cultivars. Food Sci. Technol. 42, 1605–1610. using sodium alginate and its controlled release properties. Int. J. Biol. Macromol.
Rampon, V., Riaublanc, A., Anton, M., Genot, C., McClements, D.J., 2003. Evidence 38, 25–30.
that homogenization of BSA-stabilized hexadecane-in-water emulsion induces Young, S.L., Sadra, X., Rosenberg, M., 1993. Microencapsulating properties of whey
structure modification of the nonadsorbed protein. J. Agric. Food Chem. 51, proteins. 2. Combination of whey proteins with carbohydrates. J. Dairy Sci. 76,
5900–5905. 2878–2885.
Rascon, M.P., Beristain, C.I., Garcie, H.S., Salgado, M.A., 2010. Carotenoid retention Yu, C., Wang, W., Yao, H., Liu, H., 2007. Preparation of phospholipid microcapsules
and storage stability of spray-dried paprika oleoresin using gum Arabic and soy by spray drying. Dry. Technol. 25, 695–702.
protein isolate as wall materials. Food Sci. Technol. 44, 549–557. Yu, J.Y., Lee, W.C., 1997. Microencapsulation of pyrrolnitrin from Pseu-
Raymundo, A., Gouveia, L., Batista, A.P., Empis, J., Sousa, I., 2005. Fat mimetic capacity domonas cepacia using gluten and casein. J. Ferment. Bioeng. 84,
of Chlorella vulgaris biomass in oil-in-water food emulsions stabilized by pea 444–448.
protein. Food Res. Int. 38, 961–965. Zhong, Q., Jin, M., Davidson, P.M., Zivanovic, S., 2009. Sustained release of lysozyme
Richard, J., Benoit, J.P., 2000. Microencapsulation. Techniques de l’Ingénieur. J. 2 from zein microcapsules produced by a supercritical anti-solvent process. Food
(210), 1–20. Chem. 115, 697–700.

Vegetable Proteins in Microencapsulation: A Review of Recent Interventions and Their Effectiveness

Uploaded by

Copyright:

Available Formats

Vegetable Proteins in Microencapsulation: A Review of Recent Interventions and Their Effectiveness

Uploaded by

Document Information

Original Title

Copyright

Available Formats

Share this document

Share or Embed Document

Sharing Options

Did you find this document useful?

Is this content inappropriate?

Copyright:

Available Formats

Vegetable Proteins in Microencapsulation: A Review of Recent Interventions and Their Effectiveness

Uploaded by

Copyright:

Available Formats

Industrial Crops and Products 42 (2013) 469–479

Contents lists available at SciVerse ScienceDirect

Industrial Crops and Products

Vegetable proteins in microencapsulation: A review of recent interventions and

3.1. Soy proteins

Microencapsulation process Wall material Core material Reference

Spray-drying SPI Orange oil Kim et al. (1996)

2/1 35 1.52 – Kim et al. (1996)

Microencapsulation process Wall material Core material Reference

Pea proteins ␣-Tocopherol 2.2 86.8 28 Pierucci et al. (2007)

Microencapsulation process Wall material Core material Reference

5. Conclusions and future prospects References

You might also like