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Mohammad Zarei

Universiti Teknologi Mara, Food Science and Technology, Faculty Member

UPM - Universiti Putra Malaysia, Faculty of Food Science and Tachnology, Post-Doc

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I am currently working as Senior Lecturer at University Technology MARA (UiTM), Shah Alam, Malaysia. I was. a postdoctoral researcher at the Faculty of Food Science and Technology, Universiti Putra Malaysia (2016-2019). I do research in Food Science and Biotechnology fields. My research interests now are bioactive compounds: Extraction, characterization, and identification of bioactive compounds from plant and animal sources, application and incorporation of bioactive compounds in food systems, improvement of bioaccessibility and bioavailability of bioactive compounds as well as functional food and nutraceuticals: Isolation, characterization and biological activity of peptides derived from enzymatic hydrolysis of food proteins and their structure-activity relationships.
Address: Department of Food Science and Technology, School of Industrial Technology
Faculty of Applied Sciences, Universiti Teknologi MARA (UiTM)

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Papers by Mohammad Zarei

Sorghum as a Potential Valuable Aquafeed Ingredient: Nutritional Quality and Digestibility

Agriculture

The world population is increasing, and our current agricultural practices are not sustainable en... more The world population is increasing, and our current agricultural practices are not sustainable enough to address the concerns. Alternative proteins including plant-based proteins would provide a more sustainable source of food and feed ingredients. Among food systems, the aquaculture industry is rapidly growing, while still depending on marine sources as a main source of protein. Thus, using alternative plant-based proteins as a source for developing aquafeed would make this industry more viable. Sorghum is a valuable grain with high protein contents, proper mineral and fatty acids balance, and is available all around the world. However, sorghum has not been used widely for aquafeed development. In this review article, we cover sorghum production, composition, sorghum as a protein source for aquafeed development, and bioprocessing methods for enhancing the quality of sorghum.

Whey Protein Concentrate as a Novel Source of Bifunctional Peptides with Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Properties: RSM Study

Foods, 2020

Whey protein concentrate (WPC) is a unique source of protein with numerous nutritional and functi... more Whey protein concentrate (WPC) is a unique source of protein with numerous nutritional and functional values due to the high content of branched-chain amino acid. This study was designed to establish the optimum conditions for Alcalase-hydrolysis of WPC to produce protein hydrolysates with dual biofunctionalities of angiotensin-I converting enzyme (ACE) inhibitory and antioxidant activities via response surface methodology (RSM). The results showed that the optimum conditions were achieved at temperature = 58.2 °C, E/S ratio = 2.5%, pH = 7.5 and hydrolysis time = 361.8 min in order to obtain the maximum DH (89.2%), ACE-inhibition (98.4%), DPPH• radical scavenging activity (50.1%) and ferrous ion chelation (73.1%). The well-fitted experimental data to predicted data further validates the regression model adequacy. Current study demonstrates the potential of WPC to generate bifunctional hydrolysates with ACE inhibition and antioxidant activity. This finding fosters the use of WPC hydr...

Potentiality of Self-Cloned Lactobacillus plantarum Taj-Apis362 for Enhancing GABA Production in Yogurt under Glucose Induction: Optimization and Its Cardiovascular Effect on Spontaneous Hypertensive Rats

Foods, 2020

The current study evaluated the γ-aminobutyric acid (GABA) producing ability from three novel str... more The current study evaluated the γ-aminobutyric acid (GABA) producing ability from three novel strains of lactic acid bacteria (L. plantarum Taj-Apis362, assigned as UPMC90, UPMC91, and UPMC1065) co-cultured with starter culture in a yogurt. A combination of UPMC90 + UPMC91 with starter culture symbiotically revealed the most prominent GABA-producing effect. Response surface methodology revealed the optimized fermentation conditions at 39.0 °C, 7.25 h, and 11.5 mM glutamate substrate concentration to produce GABA-rich yogurt (29.96 mg/100 g) with desirable pH (3.93) and water-holding capacity (63.06%). At 2% glucose to replace pyridoxal-5-phosphate (PLP), a cofactor typically needed during GABA production, GABA content was further enhanced to 59.00 mg/100 g. In vivo study using this sample revealed a blood pressure-lowering efficacy at 0.1 mg/kg GABA dosage (equivalent to 30 mg/kg GABA-rich yogurt) in spontaneously hypertensive rats. An improved method to produce GABA-rich yogurt has...

Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives

Food Control, 2019

Kenaf seeds are a promising source of natural preservatives for food applications due to their po... more Kenaf seeds are a promising source of natural preservatives for food applications due to their potential as a substrate to generate peptides with high antibacterial activity. We sought to generate bioactive peptides with antibacterial activity from Kenaf seed proteins via lactofermentation. The ground seeds were defatted and protein extracted using acid precipitation. Kenaf seed protein was fermented with Lactobacillus casei for 72 h at 37 °C, and the antibacterial activity, MIC, and MBC were determined using a 96-well microtiter plate assay. The fermented protein was subjected to fractionation and peptide identification using reversedphase high pressure liquid chromatography and liquid chromatography-mass spectrometry, respectively. The fermented protein showed high antibacterial activity against Salmonella typhimurim, Escherichia coli, Psedomonas aerginosa, Staphylococcus aureus, Bacilus subtilis, and Streptococcus pyogenes. The MIC value was 4 mg/mL against all tested pathogens and the MBC value was 8 mg/mL against S. typhimurium, P. aureginosa, and E. coli and 4 mg/mL against B. subtilis, S. aureus, and S. pyogenes. Fraction 17 demonstrated the strongest antibacterial activity (98%-100%), and five peptides sequences were identified in this fraction. The findings of this study demonstrated high potential for kenaf seed protein fermented using Lactobacillus casei as a source of natural preservatives for a broad range of food applications.

Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins

Biomolecules, 2019

Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysat... more Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies. Results showed that the peptides were degraded at different cleavage degrees of 94%, 67% and 97% for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE. YLLLK was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and GVQEGAGHYALL (increased ACE-inhibitory activity). YLLLK showed the lowest Ki (1.51 mM) in inhibition kinetics study when compared to WAFS and GVQEGAGHYALL with Ki of 2 mM and 3.18 mM, respectively. In addition, ACE revealed the lowest K m app and V max app and higher catalytic efficiency (CE) in the presence of YLLLK at different concentrations, implying that the enzyme catalysis decreased and hence the inhibition mode increased. Furthermore, YLLLK s...

Alcalase-generated proteolysates of stone fish (Actinopyga lecanora) flesh as a new source of antioxidant peptides

International Journal of Food Properties, 2018

In the present study, the alcalase-generated proteolysates obtained after 8 h of proteolysis of s... more In the present study, the alcalase-generated proteolysates obtained after 8 h of proteolysis of stone fish flesh showed the most potent antioxidant activity in terms of DPPH • radical scavenging activity (77.43%, IC 50 of 0.5 mg/mL), ABTS • radical scavenging activity (92.73%, IC 50 of 0.33 mg/ mL) and FRAP value (39.2 mmol/100 mL FeSO 4). These proteolysates profiled and characterized as antioxidative peptides. The proteolysates were initially subjected to ultrafiltration using MWCO Spin-X UF. Potent fractions were further characterized based on hydrophobicity using reversed-phase high-performance liquid chromatography (RP-HPLC) and isoelectric point using an OFFGEL isoelectric focusing fractionator. Results indicated that most of the antioxidative peptides found in fractions with a molecular weight (MW) of less than 2 kDa, hydrophilic (hydrophilicity >80%) and basic (pI = 9.7). The final purified fraction with the highest antioxidant activity was selected for peptide identification and sequencing using Q-TOF mass spectrometry. A total of four peptides were identified, from which Peptide 1 (GVSGLHID) showed the highest antioxidant activity and this has potential as a novel bioingredient of nutraceuticals and functional foods to promote human health.

Enhanced physicochemical stability and efficacy of angiotensin I-converting enzyme (ACE) - inhibitory biopeptides by chitosan nanoparticles optimized using Box-Behnken design

Scientific reports, Jan 10, 2018

Bromelain-generated biopeptides from stone fish protein exhibit strong inhibitory effect against ... more Bromelain-generated biopeptides from stone fish protein exhibit strong inhibitory effect against ACE and can potentially serve as designer food (DF) with blood pressure lowering effect. Contextually, the DF refer to the biopeptides specifically produced to act as ACE-inhibitors other than their primary role in nutrition and can be used in the management of hypertension. However, the biopeptides are unstable under gastrointestinal tract (GIT) digestion and need to be stabilized for effective oral administration. In the present study, the stone fish biopeptides (SBs) were stabilized by their encapsulation in sodium tripolyphosphate (TPP) cross-linked chitosan nanoparticles produced by ionotropic gelation method. The nanoparticles formulation was then optimized via Box-Behnken experimental design to achieve smaller particle size (162.70 nm) and high encapsulation efficiency (75.36%) under the optimum condition of SBs:Chitosan mass ratio (0.35), homogenization speed (8000 rpm) and homog...

Improved In Vivo Efficacy of Anti-Hypertensive Biopeptides Encapsulated in Chitosan Nanoparticles Fabricated by Ionotropic Gelation on Spontaneously Hypertensive Rats

Nanomaterials (Basel, Switzerland), Jan 2, 2017

Recent biotechnological advances in the food industry have led to the enzymatic production of ang... more Recent biotechnological advances in the food industry have led to the enzymatic production of angiotensin I-converting enzyme (ACE)-inhibitory biopeptides with a strong blood pressure lowering effect from different food proteins. However, the safe oral administration of biopeptides is impeded by their enzymatic degradation due to gastrointestinal digestion. Consequently, nanoparticle (NP)-based delivery systems are used to overcome these gastrointestinal barriers to maintain the improved bioavailability and efficacy of the encapsulated biopeptides. In the present study, the ACE-inhibitory biopeptides were generated from stone fish () protein using bromelain and stabilized by their encapsulation in chitosan (chit) nanoparticles (NPs). The nanoparticles were characterized for in vitro physicochemical properties and their antihypertensive effect was then evaluated on spontaneously hypertensive rats (SHRs). The results of a physicochemical characterization showed a small particle size o...

High angiotensin-I converting enzyme (ACE) inhibitory activity of Alcalase-digested green soybean (Glycine max) hydrolysates

Food research international (Ottawa, Ont.), 2018

As a protein-rich, underutilized crop, green soybean could be exploited to produce hydrolysates c... more As a protein-rich, underutilized crop, green soybean could be exploited to produce hydrolysates containing angiotensin-I converting enzyme (ACE) inhibitory peptides. Defatted green soybean was hydrolyzed using four different food-grade proteases (Alcalase, Papain, Flavourzyme and Bromelain) and their ACE inhibitory activities were evaluated. The Alcalase-generated green soybean hydrolysate showed the highest ACE inhibitory activity (IC: 0.14 mg/mL at 6 h hydrolysis time) followed by Papain (IC: 0.20 mg/mL at 5 h hydrolysis time), Bromelain (IC: 0.36 mg/mL at 6 h hydrolysis time) and Flavourzyme (IC: 1.14 mg/mL at 6 h hydrolysis time) hydrolysates. The Alcalase-generated hydrolysate was profiled based on its hydrophobicity and isoelectric point using reversed phase high performance liquid chromatography (RP-HPLC) and isoelectric point focusing (IEF) fractionators. The Alcalase-generated green soybean hydrolysate comprising of peptides EAQRLLF, PSLRSYLAE, PDRSIHGRQLAE, FITAFR and RGQV...

Optimization of Bromelain-Aided Production of Angiotensin I-Converting Enzyme Inhibitory Hydrolysates from Stone Fish Using Response Surface Methodology

Marine drugs, Jan 31, 2017

The stone fish is an under-utilized sea cucumber with many nutritional and ethno-medicinal values... more The stone fish is an under-utilized sea cucumber with many nutritional and ethno-medicinal values. This study aimed to establish the conditions for its optimum hydrolysis with bromelain to generate angiotensin I-converting enzyme (ACE)-inhibitory hydrolysates. Response surface methodology (RSM) based on a central composite design was used to model and optimize the degree of hydrolysis (DH) and ACE-inhibitory activity. Process conditions including pH (4-7), temperature (40-70 °C), enzyme/substrate (E/S) ratio (0.5%-2%) and time (30-360 min) were used. A pH of 7.0, temperature of 40 °C, E/S ratio of 2% and time of 240 min were determined using a response surface model as the optimum levels to obtain the maximum ACE-inhibitory activity of 84.26% at 44.59% degree of hydrolysis. Hence, RSM can serve as an effective approach in the design of experiments to improve the antihypertensive effect of stone fish hydrolysates, which can thus be used as a value-added ingredient for various applica...

Production of Defatted Palm Kernel Cake Protein Hydrolysate as a Valuable Source of Natural Antioxidants

International Journal of Molecular Sciences, 2012

The aim of this study was to produce a valuable protein hydrolysate from palm kernel cake (PKC) f... more The aim of this study was to produce a valuable protein hydrolysate from palm kernel cake (PKC) for the development of natural antioxidants. Extracted PKC protein was hydrolyzed using different proteases (alcalase, chymotrypsin, papain, pepsin, trypsin, flavourzyme, and bromelain). Subsequently, antioxidant activity and degree of hydrolysis (DH) of each hydrolysate were evaluated using DPPH• radical scavenging activity and O-phthaldialdehyde spectrophotometric assay, respectively. The results revealed a strong correlation between DH and radical scavenging activity of the hydrolysates, where among these, protein hydrolysates produced by papain after 38 h hydrolysis exhibited the highest DH (91 ± 0.1%) and DPPH• radical scavenging activity (73.5 ± 0.25%) compared to the other hydrolysates. In addition, fractionation of the most effective (potent) hydrolysate by reverse phase high performance liquid chromatography indicated a direct association between hydrophobicity and radical scavenging activity of the hydrolysates. Isoelectric focusing tests also revealed that protein hydrolysates with basic and neutral isoelectric point (pI) have the highest radical scavenging activity, although few fractions in the acidic range also exhibited good antioxidant potential.

Angiotensin I converting enzyme (ACE) inhibitory peptide derived from the sauce of fermented blue mussel

Bioresource Technology, 2005

The angiotensin I converting enzyme (ACE) inhibitory activity of fermented blue mussel sauce (FBM... more The angiotensin I converting enzyme (ACE) inhibitory activity of fermented blue mussel sauce (FBMS) was investigated. Blue mussels were fermented with 25% NaCl (w/w) at 20 degrees C for 6 months and the resultant mixture was passed through a 40-mesh sieve, desalted using an electrodialyzer and then lyophilized. The IC(50) value of FBMS for ACE activity was 1.01 mg/ml. An ACE inhibitory peptide was purified from FBMS using Sephadex G-75 gel chromatography, SP-Sephadex C-25 ion exchange chromatography and reversed-phase high-performance liquid chromatography on a C(18) column. The IC(50) value of purified ACE inhibitory peptide was 19.34 microg/ml, and 10 amino acid residues of the N-terminal sequence was EVMAGNLYPG. The purified peptide was evaluated for antihypertensive effect in spontaneously hypertensive rats (SHR) following oral administration. Blood pressure significantly decreased after peptide ingestion. This result suggested that FBMS may have beneficial effects on hypertension.

Identification and characterization of papain-generated antioxidant peptides from palm kernel cake proteins

Food Research International, 2014

Novel peptides with antioxidant activity were isolated and identified from papain generated palm ... more Novel peptides with antioxidant activity were isolated and identified from papain generated palm kernel cake (PKC) proteolysate. The proteolysate was fractionated into individual peptides based on hydrophobicity and isoelectric point using reversed-phase highperformance liquid chromatography and isoelectric focusing techniques. The individual peptides were identified by tandem mass spectrometry and their respective antioxidant activities were evaluated using 2,2-diphenyl-1-picrylhydrazyl radical scavenging activity and metal chelating activity assays. Peptide sequences, AWFS, WAF, and LPWRPATNVF showed the highest radical scavenging activities of 71%, 56%, and 50%, respectively, while peptide sequences GGIF, YGIKVGYAIP and YLLLK showed the highest metal chelating activities of 56%, 53%, and 50%, respectively. However, the best IC50 values of peptides measured by DPPHradical dot assay were displayed by GIFE, GVQEGAGHYALL and GGIF at 0.02 μM, 0.09 μM and 0.35 μM, respectively, while the best half maximal inhibitory concentration values measured using metal chelating activity were shown by LPWRPATNVF, AWFS and YGIKVGYAIP at 0.001 μM, 0.002 μM and 0.087 μM, respectively. It can be concluded that the peptides derived from PKC proteolysate were more potent and distinctive compared to those previously reported from other plant protein sources.

Evaluation of the functional properties of mung bean protein isolate for development of textured vegetable protein

Mung bean is considered a ‘green pearl’ for its relatively high protein content; however, it has ... more Mung bean is considered a ‘green pearl’ for its relatively high protein content; however, it has limited application as a raw material for industrial food products. As the potential use of mung beans relies on its protein behavior, this study characterized the functional properties of mung bean protein isolates and the results were compared with soy protein isolates. The protein isolates were prepared from mung bean and soy bean flours via extraction with 1 N NaOH, precipitated at pH 4, and subsequently freeze-dried. The amino acid profile as well as the hydrophilic and hydrophobic ratio of mung bean protein isolate, had been comparable with soy protein isolate. The water and oil absorption capacities as well as the denaturation temperature of mung bean protein isolate, were found to be similar with those of soy bean protein isolate. However, foaming capacity (89.66%) of mung bean protein isolate was higher than that of soy protein isolate (68.66%). Besides, least gelation concentra...

Response Surface Optimisation for the Production of Antioxidant Hydrolysates from Stone Fish Protein Using Bromelain

Evidence-based complementary and alternative medicine : eCAM, 2017

Protein hydrolysates produced from different food sources exhibit therapeutic potential and can b... more Protein hydrolysates produced from different food sources exhibit therapeutic potential and can be used in the management of chronic diseases. This study was targeted to optimise the conditions for the hydrolysis of stone fish protein to produce antioxidant hydrolysates using central composite design (CCD) by response surface methodology (RSM). The stone fish protein was hydrolysed under the optimum predicted conditions defined by pH (6.5), temperature (54°C), E/S ratio (1.5%), and hydrolysis time (360 min). The hydrolysates were then evaluated for 2,2-diphenyl-1-picrylhydrazyl radical (DPPH•) scavenging activity and ferrous ion- (Fe2+-) chelating activity. Results validation showed no significant difference between the experimental values of DPPH• scavenging activity (48.94%) and Fe2+-chelating activity (25.12%) obtained at 54.62% degree of hydrolysis (DH) compared to their corresponding predicted values of 49.79% and 24.08% at 53.08% DH, respectively. The hydrolysates demonstrated...

Generation, Fractionation, and Characterization of Iron-Chelating Protein Hydrolysate from Palm Kernel Cake Proteins

Journal of Food Science, 2015

Palm kernel cake protein was hydrolyzed with different proteases namely papain, bromelain, subtil... more Palm kernel cake protein was hydrolyzed with different proteases namely papain, bromelain, subtilisin, flavourzyme, trypsin, chymotrypsin, and pepsin to generate different protein hydrolysates. Peptide content and iron-chelating activity of each hydrolysate were evaluated using O-phthaldialdehyde-based spectrophotometric method and ferrozine-based colorimetric assay, respectively. The results revealed a positive correlation between peptide contents and iron-chelating activities of the protein hydrolysates. Protein hydrolysate generated by papain exhibited the highest peptide content of 10.5 mM and highest iron-chelating activity of 64.8% compared with the other hydrolysates. Profiling of the papain-generated hydrolysate by reverse phase high performance liquid chromatography fractionation indicated a direct association between peptide content and iron-chelating activity in most of the fractions. Further fractionation using isoelectric focusing also revealed that protein hydrolysate with basic and neutral isoelectric point (pI) had the highest iron-chelating activity, although a few fractions in the acidic range also exhibited good metal chelating potential. After identification and synthesis of papain-generated peptides, GGIF and YLLLK showed among the highest iron-chelating activities of 56% and 53%, whereas their IC50 were 1.4 and 0.2 μM, respectively.

Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives

Kenaf seeds are a promising source of natural preservatives for food applications due to their po... more Kenaf seeds are a promising source of natural preservatives for food applications due to their potential as a substrate to generate peptides with high antibacterial activity. We sought to generate bioactive peptides with antibacterial activity from Kenaf seed proteins via lacto-fermentation. The ground seeds were defatted and protein extracted using acid precipitation. Kenaf seed protein was fermented with Lactobacillus casei for 72 h at 37°C, and the antibacterial activity, MIC, and MBC were determined using a 96-well microtiter plate assay. The fermented protein was subjected to fractionation and peptide identification using reversed-phase high pressure liquid chromatography and liquid chromatography-mass spectrometry, respectively. The fermented protein showed high antibacterial activity against Salmonella typhimurim, Escherichia coli, Psedomonas aerginosa, Staphylococcus aureus, Bacilus subtilis, and Streptococcus pyogenes. The MIC value was 4 mg/mL against all tested pathogens and the MBC value was 8 mg/mL against S. typhimurium, P. aureginosa, and E. coli and 4 mg/mL against B. subtilis, S. aureus, and S. pyogenes. Fraction 17 demonstrated the strongest antibacterial activity (98%-100%), and five peptides sequences were identified in this fraction. The findings of this study demonstrated high potential for kenaf seed protein fermented using Lactobacillus casei as a source of natural preservatives for a broad range of food applications.

Effects of Storage Time and Temperature on Lipid Oxidation and Protein Co-Oxidation of Low-Moisture Shredded Meat Products

by Mohammad Zarei and Wan Zunairah Wan Ibadullah

Studies on the oxidative changes in meat-based, low-moisture, ready to eat foods are complicated ... more Studies on the oxidative changes in meat-based, low-moisture, ready to eat foods are complicated due to complex food system and slow lipid-protein oxidative deterioration. The current study evaluates the oxidative changes over six months of storage on shredded beef and chicken products (locally known as serunding) for physicochemical analysis, lipid oxidation (conjugated dienes and malondialdehydes) and protein co-oxidation (soluble protein content, amino acid composition, protein carbonyl, tryptophan loss and Schiff base fluorescence) at 25 • C, 40 • C and 60 • C. The lipid stability of chicken serunding was significantly lower than beef serunding, illustrated by higher conjugated dienes content and higher rate of malondialdehyde formation during storage. In terms of protein co-oxidation, chicken serunding with higher polyunsaturated fatty acids (PUFA) experienced more severe oxidation, as seen from lower protein solubility, higher protein carbonyl and Schiff base formation compared to beef serunding. To conclude, chicken serunding demonstrates lower lipid and protein stability and exhibits higher rate of lipid oxidation and protein co-oxidation than beef serunding. These findings provide insights on the progression of lipid oxidation and protein co-oxidation in cooked, shredded meat products and could be extrapolated to minimize possible adverse effects arising from lipid oxidation and protein co-oxidation, on the quality of low-moisture, high-lipid, high-protein foods.

Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins

by DR ADI MD SIKIN and Mohammad Zarei

Biomolecules, 2019

Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysat... more Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against
angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies.
Results showed that the peptides were degraded at different cleavage degrees of 94%, 67% and 97%
for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE. YLLLK
was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and
GVQEGAGHYALL (increased ACE-inhibitory activity). YLLLK showed the lowest Ki (1.51 mM) in
inhibition kinetics study when compared to WAFS and GVQEGAGHYALL with Ki of 2 mM and
3.18 mM, respectively. In addition, ACE revealed the lowest 𝐾􀭫
􀭟􀭮􀭮
and 𝑉􀭫􀭟􀭶
􀭟􀭮􀭮
and higher catalytic
efficiency (CE) in the presence of YLLLK at different concentrations, implying that the enzyme
catalysis decreased and hence the inhibition mode increased. Furthermore, YLLLK showed the
lowest docking score of −8.224 and seven interactions with tACE, while peptide GVQEGAGHYALL
showed the higher docking score of −7.006 and five interactions with tACE

Effect of microwave-assisted extraction on the yield and quality of apple pomace and lemon peel pectins

International Food Research, 2017

Microwave assisted extraction treatments showed the higher pectin yields of 10.07% and 8.83% in p... more Microwave assisted extraction treatments showed the higher pectin yields of 10.07% and 8.83% in pretreated samples by microwave and 9.4% and 8% in the extraction of dried after microwave treatment in lemon peel and apple pomace samples, respectively. Lemon peel pectin in pretreated samples by microwave and extraction of dried after microwave treatment showed the higher degree of esterification 71.8% and 70%, respectively, while apple pomace revealed 68% and 65.4% in same treatments. Furthermore, lemon peel pectin exhibited the highest galacturonic content of 74.5% in extraction of pretreated samples by microwave, while apple pomace pectin indicated the higher galacturonic acid content of 70.5% and 70% in both extraction of dried after microwave treatment and extraction of dried samples. Texture analysis of jellies prepared by various extracted pectin indicated the highest fracturability in the microwave-assisted drying treatment of 33 N and 32.5 N for apple pomace and lemon peel pectin, respectively.

Sorghum as a Potential Valuable Aquafeed Ingredient: Nutritional Quality and Digestibility

Agriculture

The world population is increasing, and our current agricultural practices are not sustainable en... more The world population is increasing, and our current agricultural practices are not sustainable enough to address the concerns. Alternative proteins including plant-based proteins would provide a more sustainable source of food and feed ingredients. Among food systems, the aquaculture industry is rapidly growing, while still depending on marine sources as a main source of protein. Thus, using alternative plant-based proteins as a source for developing aquafeed would make this industry more viable. Sorghum is a valuable grain with high protein contents, proper mineral and fatty acids balance, and is available all around the world. However, sorghum has not been used widely for aquafeed development. In this review article, we cover sorghum production, composition, sorghum as a protein source for aquafeed development, and bioprocessing methods for enhancing the quality of sorghum.

Whey Protein Concentrate as a Novel Source of Bifunctional Peptides with Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Properties: RSM Study

Foods, 2020

Whey protein concentrate (WPC) is a unique source of protein with numerous nutritional and functi... more Whey protein concentrate (WPC) is a unique source of protein with numerous nutritional and functional values due to the high content of branched-chain amino acid. This study was designed to establish the optimum conditions for Alcalase-hydrolysis of WPC to produce protein hydrolysates with dual biofunctionalities of angiotensin-I converting enzyme (ACE) inhibitory and antioxidant activities via response surface methodology (RSM). The results showed that the optimum conditions were achieved at temperature = 58.2 °C, E/S ratio = 2.5%, pH = 7.5 and hydrolysis time = 361.8 min in order to obtain the maximum DH (89.2%), ACE-inhibition (98.4%), DPPH• radical scavenging activity (50.1%) and ferrous ion chelation (73.1%). The well-fitted experimental data to predicted data further validates the regression model adequacy. Current study demonstrates the potential of WPC to generate bifunctional hydrolysates with ACE inhibition and antioxidant activity. This finding fosters the use of WPC hydr...

Potentiality of Self-Cloned Lactobacillus plantarum Taj-Apis362 for Enhancing GABA Production in Yogurt under Glucose Induction: Optimization and Its Cardiovascular Effect on Spontaneous Hypertensive Rats

Foods, 2020

The current study evaluated the γ-aminobutyric acid (GABA) producing ability from three novel str... more The current study evaluated the γ-aminobutyric acid (GABA) producing ability from three novel strains of lactic acid bacteria (L. plantarum Taj-Apis362, assigned as UPMC90, UPMC91, and UPMC1065) co-cultured with starter culture in a yogurt. A combination of UPMC90 + UPMC91 with starter culture symbiotically revealed the most prominent GABA-producing effect. Response surface methodology revealed the optimized fermentation conditions at 39.0 °C, 7.25 h, and 11.5 mM glutamate substrate concentration to produce GABA-rich yogurt (29.96 mg/100 g) with desirable pH (3.93) and water-holding capacity (63.06%). At 2% glucose to replace pyridoxal-5-phosphate (PLP), a cofactor typically needed during GABA production, GABA content was further enhanced to 59.00 mg/100 g. In vivo study using this sample revealed a blood pressure-lowering efficacy at 0.1 mg/kg GABA dosage (equivalent to 30 mg/kg GABA-rich yogurt) in spontaneously hypertensive rats. An improved method to produce GABA-rich yogurt has...

Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives

Food Control, 2019

Kenaf seeds are a promising source of natural preservatives for food applications due to their po... more Kenaf seeds are a promising source of natural preservatives for food applications due to their potential as a substrate to generate peptides with high antibacterial activity. We sought to generate bioactive peptides with antibacterial activity from Kenaf seed proteins via lactofermentation. The ground seeds were defatted and protein extracted using acid precipitation. Kenaf seed protein was fermented with Lactobacillus casei for 72 h at 37 °C, and the antibacterial activity, MIC, and MBC were determined using a 96-well microtiter plate assay. The fermented protein was subjected to fractionation and peptide identification using reversedphase high pressure liquid chromatography and liquid chromatography-mass spectrometry, respectively. The fermented protein showed high antibacterial activity against Salmonella typhimurim, Escherichia coli, Psedomonas aerginosa, Staphylococcus aureus, Bacilus subtilis, and Streptococcus pyogenes. The MIC value was 4 mg/mL against all tested pathogens and the MBC value was 8 mg/mL against S. typhimurium, P. aureginosa, and E. coli and 4 mg/mL against B. subtilis, S. aureus, and S. pyogenes. Fraction 17 demonstrated the strongest antibacterial activity (98%-100%), and five peptides sequences were identified in this fraction. The findings of this study demonstrated high potential for kenaf seed protein fermented using Lactobacillus casei as a source of natural preservatives for a broad range of food applications.

Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins

Biomolecules, 2019

Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysat... more Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies. Results showed that the peptides were degraded at different cleavage degrees of 94%, 67% and 97% for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE. YLLLK was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and GVQEGAGHYALL (increased ACE-inhibitory activity). YLLLK showed the lowest Ki (1.51 mM) in inhibition kinetics study when compared to WAFS and GVQEGAGHYALL with Ki of 2 mM and 3.18 mM, respectively. In addition, ACE revealed the lowest K m app and V max app and higher catalytic efficiency (CE) in the presence of YLLLK at different concentrations, implying that the enzyme catalysis decreased and hence the inhibition mode increased. Furthermore, YLLLK s...

Alcalase-generated proteolysates of stone fish (Actinopyga lecanora) flesh as a new source of antioxidant peptides

International Journal of Food Properties, 2018

In the present study, the alcalase-generated proteolysates obtained after 8 h of proteolysis of s... more In the present study, the alcalase-generated proteolysates obtained after 8 h of proteolysis of stone fish flesh showed the most potent antioxidant activity in terms of DPPH • radical scavenging activity (77.43%, IC 50 of 0.5 mg/mL), ABTS • radical scavenging activity (92.73%, IC 50 of 0.33 mg/ mL) and FRAP value (39.2 mmol/100 mL FeSO 4). These proteolysates profiled and characterized as antioxidative peptides. The proteolysates were initially subjected to ultrafiltration using MWCO Spin-X UF. Potent fractions were further characterized based on hydrophobicity using reversed-phase high-performance liquid chromatography (RP-HPLC) and isoelectric point using an OFFGEL isoelectric focusing fractionator. Results indicated that most of the antioxidative peptides found in fractions with a molecular weight (MW) of less than 2 kDa, hydrophilic (hydrophilicity >80%) and basic (pI = 9.7). The final purified fraction with the highest antioxidant activity was selected for peptide identification and sequencing using Q-TOF mass spectrometry. A total of four peptides were identified, from which Peptide 1 (GVSGLHID) showed the highest antioxidant activity and this has potential as a novel bioingredient of nutraceuticals and functional foods to promote human health.

Enhanced physicochemical stability and efficacy of angiotensin I-converting enzyme (ACE) - inhibitory biopeptides by chitosan nanoparticles optimized using Box-Behnken design

Scientific reports, Jan 10, 2018

Bromelain-generated biopeptides from stone fish protein exhibit strong inhibitory effect against ... more Bromelain-generated biopeptides from stone fish protein exhibit strong inhibitory effect against ACE and can potentially serve as designer food (DF) with blood pressure lowering effect. Contextually, the DF refer to the biopeptides specifically produced to act as ACE-inhibitors other than their primary role in nutrition and can be used in the management of hypertension. However, the biopeptides are unstable under gastrointestinal tract (GIT) digestion and need to be stabilized for effective oral administration. In the present study, the stone fish biopeptides (SBs) were stabilized by their encapsulation in sodium tripolyphosphate (TPP) cross-linked chitosan nanoparticles produced by ionotropic gelation method. The nanoparticles formulation was then optimized via Box-Behnken experimental design to achieve smaller particle size (162.70 nm) and high encapsulation efficiency (75.36%) under the optimum condition of SBs:Chitosan mass ratio (0.35), homogenization speed (8000 rpm) and homog...

Improved In Vivo Efficacy of Anti-Hypertensive Biopeptides Encapsulated in Chitosan Nanoparticles Fabricated by Ionotropic Gelation on Spontaneously Hypertensive Rats

Nanomaterials (Basel, Switzerland), Jan 2, 2017

Recent biotechnological advances in the food industry have led to the enzymatic production of ang... more Recent biotechnological advances in the food industry have led to the enzymatic production of angiotensin I-converting enzyme (ACE)-inhibitory biopeptides with a strong blood pressure lowering effect from different food proteins. However, the safe oral administration of biopeptides is impeded by their enzymatic degradation due to gastrointestinal digestion. Consequently, nanoparticle (NP)-based delivery systems are used to overcome these gastrointestinal barriers to maintain the improved bioavailability and efficacy of the encapsulated biopeptides. In the present study, the ACE-inhibitory biopeptides were generated from stone fish () protein using bromelain and stabilized by their encapsulation in chitosan (chit) nanoparticles (NPs). The nanoparticles were characterized for in vitro physicochemical properties and their antihypertensive effect was then evaluated on spontaneously hypertensive rats (SHRs). The results of a physicochemical characterization showed a small particle size o...

High angiotensin-I converting enzyme (ACE) inhibitory activity of Alcalase-digested green soybean (Glycine max) hydrolysates

Food research international (Ottawa, Ont.), 2018

As a protein-rich, underutilized crop, green soybean could be exploited to produce hydrolysates c... more As a protein-rich, underutilized crop, green soybean could be exploited to produce hydrolysates containing angiotensin-I converting enzyme (ACE) inhibitory peptides. Defatted green soybean was hydrolyzed using four different food-grade proteases (Alcalase, Papain, Flavourzyme and Bromelain) and their ACE inhibitory activities were evaluated. The Alcalase-generated green soybean hydrolysate showed the highest ACE inhibitory activity (IC: 0.14 mg/mL at 6 h hydrolysis time) followed by Papain (IC: 0.20 mg/mL at 5 h hydrolysis time), Bromelain (IC: 0.36 mg/mL at 6 h hydrolysis time) and Flavourzyme (IC: 1.14 mg/mL at 6 h hydrolysis time) hydrolysates. The Alcalase-generated hydrolysate was profiled based on its hydrophobicity and isoelectric point using reversed phase high performance liquid chromatography (RP-HPLC) and isoelectric point focusing (IEF) fractionators. The Alcalase-generated green soybean hydrolysate comprising of peptides EAQRLLF, PSLRSYLAE, PDRSIHGRQLAE, FITAFR and RGQV...

Optimization of Bromelain-Aided Production of Angiotensin I-Converting Enzyme Inhibitory Hydrolysates from Stone Fish Using Response Surface Methodology

Marine drugs, Jan 31, 2017

The stone fish is an under-utilized sea cucumber with many nutritional and ethno-medicinal values... more The stone fish is an under-utilized sea cucumber with many nutritional and ethno-medicinal values. This study aimed to establish the conditions for its optimum hydrolysis with bromelain to generate angiotensin I-converting enzyme (ACE)-inhibitory hydrolysates. Response surface methodology (RSM) based on a central composite design was used to model and optimize the degree of hydrolysis (DH) and ACE-inhibitory activity. Process conditions including pH (4-7), temperature (40-70 °C), enzyme/substrate (E/S) ratio (0.5%-2%) and time (30-360 min) were used. A pH of 7.0, temperature of 40 °C, E/S ratio of 2% and time of 240 min were determined using a response surface model as the optimum levels to obtain the maximum ACE-inhibitory activity of 84.26% at 44.59% degree of hydrolysis. Hence, RSM can serve as an effective approach in the design of experiments to improve the antihypertensive effect of stone fish hydrolysates, which can thus be used as a value-added ingredient for various applica...

Production of Defatted Palm Kernel Cake Protein Hydrolysate as a Valuable Source of Natural Antioxidants

International Journal of Molecular Sciences, 2012

The aim of this study was to produce a valuable protein hydrolysate from palm kernel cake (PKC) f... more The aim of this study was to produce a valuable protein hydrolysate from palm kernel cake (PKC) for the development of natural antioxidants. Extracted PKC protein was hydrolyzed using different proteases (alcalase, chymotrypsin, papain, pepsin, trypsin, flavourzyme, and bromelain). Subsequently, antioxidant activity and degree of hydrolysis (DH) of each hydrolysate were evaluated using DPPH• radical scavenging activity and O-phthaldialdehyde spectrophotometric assay, respectively. The results revealed a strong correlation between DH and radical scavenging activity of the hydrolysates, where among these, protein hydrolysates produced by papain after 38 h hydrolysis exhibited the highest DH (91 ± 0.1%) and DPPH• radical scavenging activity (73.5 ± 0.25%) compared to the other hydrolysates. In addition, fractionation of the most effective (potent) hydrolysate by reverse phase high performance liquid chromatography indicated a direct association between hydrophobicity and radical scavenging activity of the hydrolysates. Isoelectric focusing tests also revealed that protein hydrolysates with basic and neutral isoelectric point (pI) have the highest radical scavenging activity, although few fractions in the acidic range also exhibited good antioxidant potential.

Angiotensin I converting enzyme (ACE) inhibitory peptide derived from the sauce of fermented blue mussel

Bioresource Technology, 2005

The angiotensin I converting enzyme (ACE) inhibitory activity of fermented blue mussel sauce (FBM... more The angiotensin I converting enzyme (ACE) inhibitory activity of fermented blue mussel sauce (FBMS) was investigated. Blue mussels were fermented with 25% NaCl (w/w) at 20 degrees C for 6 months and the resultant mixture was passed through a 40-mesh sieve, desalted using an electrodialyzer and then lyophilized. The IC(50) value of FBMS for ACE activity was 1.01 mg/ml. An ACE inhibitory peptide was purified from FBMS using Sephadex G-75 gel chromatography, SP-Sephadex C-25 ion exchange chromatography and reversed-phase high-performance liquid chromatography on a C(18) column. The IC(50) value of purified ACE inhibitory peptide was 19.34 microg/ml, and 10 amino acid residues of the N-terminal sequence was EVMAGNLYPG. The purified peptide was evaluated for antihypertensive effect in spontaneously hypertensive rats (SHR) following oral administration. Blood pressure significantly decreased after peptide ingestion. This result suggested that FBMS may have beneficial effects on hypertension.

Identification and characterization of papain-generated antioxidant peptides from palm kernel cake proteins

Food Research International, 2014

Novel peptides with antioxidant activity were isolated and identified from papain generated palm ... more Novel peptides with antioxidant activity were isolated and identified from papain generated palm kernel cake (PKC) proteolysate. The proteolysate was fractionated into individual peptides based on hydrophobicity and isoelectric point using reversed-phase highperformance liquid chromatography and isoelectric focusing techniques. The individual peptides were identified by tandem mass spectrometry and their respective antioxidant activities were evaluated using 2,2-diphenyl-1-picrylhydrazyl radical scavenging activity and metal chelating activity assays. Peptide sequences, AWFS, WAF, and LPWRPATNVF showed the highest radical scavenging activities of 71%, 56%, and 50%, respectively, while peptide sequences GGIF, YGIKVGYAIP and YLLLK showed the highest metal chelating activities of 56%, 53%, and 50%, respectively. However, the best IC50 values of peptides measured by DPPHradical dot assay were displayed by GIFE, GVQEGAGHYALL and GGIF at 0.02 μM, 0.09 μM and 0.35 μM, respectively, while the best half maximal inhibitory concentration values measured using metal chelating activity were shown by LPWRPATNVF, AWFS and YGIKVGYAIP at 0.001 μM, 0.002 μM and 0.087 μM, respectively. It can be concluded that the peptides derived from PKC proteolysate were more potent and distinctive compared to those previously reported from other plant protein sources.

Evaluation of the functional properties of mung bean protein isolate for development of textured vegetable protein

Mung bean is considered a ‘green pearl’ for its relatively high protein content; however, it has ... more Mung bean is considered a ‘green pearl’ for its relatively high protein content; however, it has limited application as a raw material for industrial food products. As the potential use of mung beans relies on its protein behavior, this study characterized the functional properties of mung bean protein isolates and the results were compared with soy protein isolates. The protein isolates were prepared from mung bean and soy bean flours via extraction with 1 N NaOH, precipitated at pH 4, and subsequently freeze-dried. The amino acid profile as well as the hydrophilic and hydrophobic ratio of mung bean protein isolate, had been comparable with soy protein isolate. The water and oil absorption capacities as well as the denaturation temperature of mung bean protein isolate, were found to be similar with those of soy bean protein isolate. However, foaming capacity (89.66%) of mung bean protein isolate was higher than that of soy protein isolate (68.66%). Besides, least gelation concentra...

Response Surface Optimisation for the Production of Antioxidant Hydrolysates from Stone Fish Protein Using Bromelain

Evidence-based complementary and alternative medicine : eCAM, 2017

Protein hydrolysates produced from different food sources exhibit therapeutic potential and can b... more Protein hydrolysates produced from different food sources exhibit therapeutic potential and can be used in the management of chronic diseases. This study was targeted to optimise the conditions for the hydrolysis of stone fish protein to produce antioxidant hydrolysates using central composite design (CCD) by response surface methodology (RSM). The stone fish protein was hydrolysed under the optimum predicted conditions defined by pH (6.5), temperature (54°C), E/S ratio (1.5%), and hydrolysis time (360 min). The hydrolysates were then evaluated for 2,2-diphenyl-1-picrylhydrazyl radical (DPPH•) scavenging activity and ferrous ion- (Fe2+-) chelating activity. Results validation showed no significant difference between the experimental values of DPPH• scavenging activity (48.94%) and Fe2+-chelating activity (25.12%) obtained at 54.62% degree of hydrolysis (DH) compared to their corresponding predicted values of 49.79% and 24.08% at 53.08% DH, respectively. The hydrolysates demonstrated...

Generation, Fractionation, and Characterization of Iron-Chelating Protein Hydrolysate from Palm Kernel Cake Proteins

Journal of Food Science, 2015

Palm kernel cake protein was hydrolyzed with different proteases namely papain, bromelain, subtil... more Palm kernel cake protein was hydrolyzed with different proteases namely papain, bromelain, subtilisin, flavourzyme, trypsin, chymotrypsin, and pepsin to generate different protein hydrolysates. Peptide content and iron-chelating activity of each hydrolysate were evaluated using O-phthaldialdehyde-based spectrophotometric method and ferrozine-based colorimetric assay, respectively. The results revealed a positive correlation between peptide contents and iron-chelating activities of the protein hydrolysates. Protein hydrolysate generated by papain exhibited the highest peptide content of 10.5 mM and highest iron-chelating activity of 64.8% compared with the other hydrolysates. Profiling of the papain-generated hydrolysate by reverse phase high performance liquid chromatography fractionation indicated a direct association between peptide content and iron-chelating activity in most of the fractions. Further fractionation using isoelectric focusing also revealed that protein hydrolysate with basic and neutral isoelectric point (pI) had the highest iron-chelating activity, although a few fractions in the acidic range also exhibited good metal chelating potential. After identification and synthesis of papain-generated peptides, GGIF and YLLLK showed among the highest iron-chelating activities of 56% and 53%, whereas their IC50 were 1.4 and 0.2 μM, respectively.

Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives

Kenaf seeds are a promising source of natural preservatives for food applications due to their po... more Kenaf seeds are a promising source of natural preservatives for food applications due to their potential as a substrate to generate peptides with high antibacterial activity. We sought to generate bioactive peptides with antibacterial activity from Kenaf seed proteins via lacto-fermentation. The ground seeds were defatted and protein extracted using acid precipitation. Kenaf seed protein was fermented with Lactobacillus casei for 72 h at 37°C, and the antibacterial activity, MIC, and MBC were determined using a 96-well microtiter plate assay. The fermented protein was subjected to fractionation and peptide identification using reversed-phase high pressure liquid chromatography and liquid chromatography-mass spectrometry, respectively. The fermented protein showed high antibacterial activity against Salmonella typhimurim, Escherichia coli, Psedomonas aerginosa, Staphylococcus aureus, Bacilus subtilis, and Streptococcus pyogenes. The MIC value was 4 mg/mL against all tested pathogens and the MBC value was 8 mg/mL against S. typhimurium, P. aureginosa, and E. coli and 4 mg/mL against B. subtilis, S. aureus, and S. pyogenes. Fraction 17 demonstrated the strongest antibacterial activity (98%-100%), and five peptides sequences were identified in this fraction. The findings of this study demonstrated high potential for kenaf seed protein fermented using Lactobacillus casei as a source of natural preservatives for a broad range of food applications.

Effects of Storage Time and Temperature on Lipid Oxidation and Protein Co-Oxidation of Low-Moisture Shredded Meat Products

by Mohammad Zarei and Wan Zunairah Wan Ibadullah

Studies on the oxidative changes in meat-based, low-moisture, ready to eat foods are complicated ... more Studies on the oxidative changes in meat-based, low-moisture, ready to eat foods are complicated due to complex food system and slow lipid-protein oxidative deterioration. The current study evaluates the oxidative changes over six months of storage on shredded beef and chicken products (locally known as serunding) for physicochemical analysis, lipid oxidation (conjugated dienes and malondialdehydes) and protein co-oxidation (soluble protein content, amino acid composition, protein carbonyl, tryptophan loss and Schiff base fluorescence) at 25 • C, 40 • C and 60 • C. The lipid stability of chicken serunding was significantly lower than beef serunding, illustrated by higher conjugated dienes content and higher rate of malondialdehyde formation during storage. In terms of protein co-oxidation, chicken serunding with higher polyunsaturated fatty acids (PUFA) experienced more severe oxidation, as seen from lower protein solubility, higher protein carbonyl and Schiff base formation compared to beef serunding. To conclude, chicken serunding demonstrates lower lipid and protein stability and exhibits higher rate of lipid oxidation and protein co-oxidation than beef serunding. These findings provide insights on the progression of lipid oxidation and protein co-oxidation in cooked, shredded meat products and could be extrapolated to minimize possible adverse effects arising from lipid oxidation and protein co-oxidation, on the quality of low-moisture, high-lipid, high-protein foods.

Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins

by DR ADI MD SIKIN and Mohammad Zarei

Biomolecules, 2019

Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysat... more Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against
angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies.
Results showed that the peptides were degraded at different cleavage degrees of 94%, 67% and 97%
for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE. YLLLK
was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and
GVQEGAGHYALL (increased ACE-inhibitory activity). YLLLK showed the lowest Ki (1.51 mM) in
inhibition kinetics study when compared to WAFS and GVQEGAGHYALL with Ki of 2 mM and
3.18 mM, respectively. In addition, ACE revealed the lowest 𝐾􀭫
􀭟􀭮􀭮
and 𝑉􀭫􀭟􀭶
􀭟􀭮􀭮
and higher catalytic
efficiency (CE) in the presence of YLLLK at different concentrations, implying that the enzyme
catalysis decreased and hence the inhibition mode increased. Furthermore, YLLLK showed the
lowest docking score of −8.224 and seven interactions with tACE, while peptide GVQEGAGHYALL
showed the higher docking score of −7.006 and five interactions with tACE

Effect of microwave-assisted extraction on the yield and quality of apple pomace and lemon peel pectins

International Food Research, 2017

Microwave assisted extraction treatments showed the higher pectin yields of 10.07% and 8.83% in p... more Microwave assisted extraction treatments showed the higher pectin yields of 10.07% and 8.83% in pretreated samples by microwave and 9.4% and 8% in the extraction of dried after microwave treatment in lemon peel and apple pomace samples, respectively. Lemon peel pectin in pretreated samples by microwave and extraction of dried after microwave treatment showed the higher degree of esterification 71.8% and 70%, respectively, while apple pomace revealed 68% and 65.4% in same treatments. Furthermore, lemon peel pectin exhibited the highest galacturonic content of 74.5% in extraction of pretreated samples by microwave, while apple pomace pectin indicated the higher galacturonic acid content of 70.5% and 70% in both extraction of dried after microwave treatment and extraction of dried samples. Texture analysis of jellies prepared by various extracted pectin indicated the highest fracturability in the microwave-assisted drying treatment of 33 N and 32.5 N for apple pomace and lemon peel pectin, respectively.