- Department of Food Science and Technology, School of Industrial Technology
Faculty of Applied Sciences, Universiti Teknologi MARA (UiTM)
Mohammad Zarei
Universiti Teknologi Mara, Food Science and Technology, Faculty Member
- I am currently working as Senior Lecturer at University Technology MARA (UiTM), Shah Alam, Malaysia. I was. a postdoc... moreI 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.edit
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... 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.
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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... 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...
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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... 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...
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Research Interests:
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... 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...
Research Interests:
Research Interests:
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... 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...
Research Interests:
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,... 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...
Research Interests:
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... 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...
Research Interests:
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... 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...
Research Interests: Chemistry, Response Surface Methodology, Medicine, RSM, Animals, and 15 moreFishes, Hydrolysate, Temperature, Enzyme, Bioactive Peptides, Antihypertensive Studies, Angiotensin Converting Enzyme, Central Composite Design, Hydrolysis, Angiotensin Converting Enzyme Inhibitors, Bromelain, Marine Drugs, Protein hydrolysates, Antihypertensive agents, and Pharmacology and pharmaceutical sciences
Research Interests: Genetics, Chemistry, Free Radicals, Chromatography, Medicine, and 15 moreFunctional Foods, Bioactive Compounds and Phytochemicals in Foos, Antioxidant, Arecaceae, Hydrolysate, Trypsin, Molecular sciences, DPPH, Hydrolysis, PLANT PROTEINS, Plant Oils, Isoelectric point, Protein hydrolysates, proteolysis, and Papain
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... 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.
Research Interests: Chemistry, Medicine, Multidisciplinary, Korea, Bivalvia, and 15 moreBlood Pressure, Animals, Peptides, Organophosphorus Compounds, Ion Exchange Chromatography, High Performance Liquid Chromatography, High Pressure Liquid Chromatography, Fermentation, Rats, Mytilus edulis, Amino Acid Sequence, Spontaneously Hypertensive Rat, Angiotensin Converting Enzyme Inhibitors, Bioresource technology, and Complex Mixtures
Research Interests:
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... 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...
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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... 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...
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Research Interests: Chemical Engineering, Food Science, Humans, Arecaceae, Peptides, and 15 moreIron, PKC, Trypsin, Spectrophotometry, High Pressure Liquid Chromatography, Bioactive Peptides, Food Sciences, Protein Hydrolysate, Hydrolysis, Palm Kernel Cake, PLANT PROTEINS, Iron Chelating Activity, Isoelectric point, Protein hydrolysates, and Papain
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... 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.
Research Interests:
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... 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
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
Research Interests:
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,... 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.
Research Interests:
Purification of lipase produced by L. mesenteroides subsp. mesenteroides ATCC 8293 was conducted for the first time using a novel aqueous two-phase system (ATPS) composed of Triton X-100 and maltitol. The partitioning of lipase was... more
Purification of lipase produced by L. mesenteroides subsp. mesenteroides ATCC 8293 was conducted for the first time using a novel aqueous two-phase system (ATPS) composed of Triton X-100 and maltitol. The partitioning of lipase was optimized according to several parameters including pH, temperature, and crude load. Results showed that lipase preferentially migrated to the Triton X-100 rich phase and optimum lipase partitioning was achieved in ATPS at TLL of 46.4% and crude load of 20% at 30 °C and pH 8, resulting in high lipase purification factor of 17.28 and yield of 94.7%. The purified lipase showed a prominent band on SDS-PAGE with an estimated molecular weight of 50 kDa. The lipase was stable at the temperature range of 30–60 °C and pH range of 6–11, however, it revealed its optimum activity at the temperature of 37 °C and pH 8. Moreover, lipase exhibited enhanced activity in the presence of non-ionic surfactants with increased activity up to 40%. Furthermore, results exhibited that metals ions such as Na+, Mg2+, K+ and Ca2+ stimulated lipase activity. This study demonstrated that this novel system could be potentially used as an alternative to traditional ATPS for the purification and recovery of enzymes since the purified lipase still possesses good process characteristics after undergoing the purification process.
Research Interests:
Liposomes are used as effective nanodelivery devices to improve the physicochemical stability and biological efficacy of the encapsulated peptides and proteins. In this study, nanoliposome composite of lipoid S75-entrapped angiotensin... more
Liposomes are used as effective nanodelivery devices to improve the physicochemical stability and biological efficacy of the encapsulated peptides and proteins. In this study, nanoliposome composite of lipoid S75-entrapped angiotensin I-converting enzyme (ACE)-inhibitory biopeptides was prepared by conventional (BLS75-CM) and direct heating (BLS75-DHM) methods. The nanoliposomes (BLS75-CM and BLS75-DHM) were stored at 4°C for 8 weeks and evaluated for physicochemical stability in terms of particle size, polydispersity index (pdi), zeta potential, and encapsulation efficiency (EE). These were also studied for residual ACE-inhibitory efficacy following their digestion under simulated gastrointestinal tract condition. The BLS75-CM was found to maintain higher physicochemical stability in terms of particle size, pdi, and zeta potential compared to BLS75-DHM. However, the BLS75-DHM indicated higher EE and efficacy with greater residual ACE-inhibitory activity of 47.37% compared to 44.18% and 36.84% that were obtained for the digested BLS75-CM and digested biopeptides without encapsulation, respectively. In vitro release study showed a cumulative biopeptides release of 66.41% and 69.00% from BLS75-CM and BLS75-DHM, respectively. The results of transmission electron microscopy showed spherical appearance of the nanoliposome capsules while Fourier Transform Infrared spectroscopy indicated the presence of ionic complexation and hydrogen bonds between the biopeptides and their phospholipid matrix.
Research Interests:
Stone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated... more
Stone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including Ala-Leu-Gly-Pro-Gln-Phe-Tyr (794.44 Da), Lys-Val-Pro-Pro-Lys-Ala (638.88 Da), Leu-Ala-Pro-Pro-Thr-Met (628.85 Da), Glu-Val-Leu-Ile-Gln (600.77 Da) and Glu-His-Pro-Val-Leu (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.310 mM, 1.440 mM and 1.680 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.
Research Interests:
Winged bean seed (WBS) is an underutilized tropical crop. The current study evaluates its potential to reduce blood pressure (BP) in spontaneously hypertensive rats and finds that it reduces BP significantly, in a dose-dependent manner.... more
Winged bean seed (WBS) is an underutilized tropical crop. The current study evaluates its potential to reduce blood pressure (BP) in spontaneously hypertensive rats and finds that it reduces BP significantly, in a dose-dependent manner. Five peptides with the sequences, RGVFPCLK, TQLDLPTQ, EPALVP, MRSVVT and DMKP, have been characterized in terms of their stability against ACE via in vitro and in silico modelling. All peptides exhibited IC50 values between 0.019 and 6.885 mM and various inhibitory modes, including substrate, prodrug and true inhibitor modes. The toxicity status of non-Current Good Manufacturing Practice (non-CGMP) peptides is evaluated and the results show that such peptides are toxic, and thus are not suitable to be tested in animals, particularly in repeated-dose studies. In short, WBS hydrolysate demonstrated in vitro ACE inhibitory properties and in vivo blood pressure lowering efficacy in rat models, fostering its potential as a functional food ingredient. Non-CGMP grade peptides are toxic and unfit for testing in animal models.
Research Interests:
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%, IC50 of 0.5 mg/mL), ABTS•... 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%, IC50 of 0.5 mg/mL), ABTS• radical scavenging activity (92.73%, IC50 of 0.33 mg/mL) and FRAP value (39.2 mmol/100 mL FeSO4). 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.
Research Interests:
Bromelain-generated biopeptides from stone fsh protein exhibit strong inhibitory efect against ACE and can potentially serve as designer food (DF) with blood pressure lowering efect. Contextually, the DF refer to the biopeptides... more
Bromelain-generated biopeptides from stone fsh protein exhibit strong inhibitory efect against ACE
and can potentially serve as designer food (DF) with blood pressure lowering efect. Contextually, the
DF refer to the biopeptides specifcally 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 efective oral administration.
In the present study, the stone fsh 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 (162.70nm) and high encapsulation efciency (75.36%) under the optimum
condition of SBs:Chitosan mass ratio (0.35), homogenization speed (8000rpm) and homogenization
time (30min). The SBs-loaded nanoparticles were characterized for morphology by transmission
electron microscopy (TEM), physicochemical stability and efcacy. The nanoparticles were then
lyophilized and analyzed using Fourier transform infra-red spectroscopy (FTIR) and X-ray difraction
(XRD). The results obtained indicated a sustained in vitro release and enhanced physicochemical
stability of the SBs-loaded nanoparticles with smaller particle size and high encapsulation efciency
following long period of storage. Moreover, the efcacy study revealed improved inhibitory efect of the
encapsulated SBs against ACE following simulated GIT digestion.
and can potentially serve as designer food (DF) with blood pressure lowering efect. Contextually, the
DF refer to the biopeptides specifcally 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 efective oral administration.
In the present study, the stone fsh 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 (162.70nm) and high encapsulation efciency (75.36%) under the optimum
condition of SBs:Chitosan mass ratio (0.35), homogenization speed (8000rpm) and homogenization
time (30min). The SBs-loaded nanoparticles were characterized for morphology by transmission
electron microscopy (TEM), physicochemical stability and efcacy. The nanoparticles were then
lyophilized and analyzed using Fourier transform infra-red spectroscopy (FTIR) and X-ray difraction
(XRD). The results obtained indicated a sustained in vitro release and enhanced physicochemical
stability of the SBs-loaded nanoparticles with smaller particle size and high encapsulation efciency
following long period of storage. Moreover, the efcacy study revealed improved inhibitory efect of the
encapsulated SBs against ACE following simulated GIT digestion.
Research Interests:
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... 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 50 : 0.14 mg/mL at 6 h hydrolysis time) followed by Papain (IC 50 : 0.20 mg/mL at 5 h hydrolysis time), Bromelain (IC 50 : 0.36 mg/mL at 6 h hydrolysis time) and Flavourzyme (IC 50 : 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 RGQVLS, revealed the highest ACE inhibitory activity of 94.19%, 99.31%, 92.92%, 101.51% and 90.40%, respectively, while their IC 50 values were 878 μM, 532 μM, 1552 μM, 1342 μM and 993 μM, respectively. It can be concluded that Alcalase-digested green soybean hydrolysates could be exploited as a source of peptides to be incorporated into functional foods with antihypertensive activity.
Research Interests:
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,... 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 (Actinopyga lecanora)
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 of 162.70 nm, a polydispersity
index (pdi) value of 0.28, a zeta potential of 48.78 mV, a high encapsulation efficiency of 75.36%,
a high melting temperature of 146.78 ◦C and an in vitro sustained release of the biopeptides.
The results of the in vivo efficacy indicated a dose-dependent blood pressure lowering effect
of the biopeptide-loaded nanoparticles that was significantly higher (p < 0.05) compared with
the un-encapsulated biopeptides. Moreover, the results of a morphological examination using
transmission electron microscopy (TEM) demonstrated the nanoparticles as homogenous and
spherical. Thus, the ACE-inhibitory biopeptides stabilized by chitosan nanoparticles can effectively
reduce blood pressure for an extended period of time in hypertensive individuals.
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 (Actinopyga lecanora)
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 of 162.70 nm, a polydispersity
index (pdi) value of 0.28, a zeta potential of 48.78 mV, a high encapsulation efficiency of 75.36%,
a high melting temperature of 146.78 ◦C and an in vitro sustained release of the biopeptides.
The results of the in vivo efficacy indicated a dose-dependent blood pressure lowering effect
of the biopeptide-loaded nanoparticles that was significantly higher (p < 0.05) compared with
the un-encapsulated biopeptides. Moreover, the results of a morphological examination using
transmission electron microscopy (TEM) demonstrated the nanoparticles as homogenous and
spherical. Thus, the ACE-inhibitory biopeptides stabilized by chitosan nanoparticles can effectively
reduce blood pressure for an extended period of time in hypertensive individuals.
Research Interests:
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... 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-(Fe 2+-) chelating activity. Results validation showed no significant difference between the experimental values of DPPH • scavenging activity (48.94%) and Fe 2+-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 non-Newtonian behavior (í µí± < 1) with stronger shear-thinning effect and higher viscosities at increasing concentration. Thus, RSM can be considered as a promising strategy to optimise the production of stone fish protein hydrolysates containing antioxidant peptides. It is hoped that this finding will enhance the potential of stone fish protein hydrolysates (SHs) as therapeutic bioactive ingredient in functional foods development.
Research Interests:
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... 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 concentration (LGC) of mung bean protein isolate (12%) was also close to LGC of soy protein isolate (14%), while the protein solubility was comparable between both the isolated proteins. The physical features of the textured mung bean were close to the commercial textured soy protein, which showed a heterogeneous and porous network like matrix when the mung bean flour was extruded to measure its potentiality to produce textured vegetable protein.all seaweed extracts. Results showed that extraction parameters had significant effect (p < 0.05) on the antioxidant compounds and antioxidant capacities of seaweed. Sargassum polycystum portrayed the most antioxidant compounds (37.41 ± 0.01 mg GAE/g DW and 4.54 ± 0.02 mg CE/g DW) and capacities (2.00 ± 0.01 µmol TEAC/g DW and 0.84 ± 0.01 µmol TEAC/g DW) amongst four species of seaweed.
Research Interests:
Actinopyga lecanora, commonly known as sea cucumber, is a rich protein source. This marine protein source was hydrolyzed using six proteases to generate anti-inflammatory hydrolysates and bioactive peptides. Bromelain hydrolysates after 1... more
Actinopyga lecanora, commonly known as sea cucumber, is a rich protein source. This marine protein source was hydrolyzed using six proteases to generate anti-inflammatory hydrolysates and bioactive peptides. Bromelain hydrolysates after 1 h hydrolysis exhibited the highest nitric oxide (NO) inhibitory activity reflecting anti-inflammatory activity. A sequence of two fractionation methods was employed to fractionate the peptides based on their hydrophobicity using a semi-preparative RP-HPLC and isoelectric points using isoelectric focusing technique. Based on these fractionation methods, basic peptides with relatively higher hydrophobicity provided higher NO-inhibitory activity than did acidic peptides. Furthermore, using Q-TOF mass spectrometry; 12 peptide sequences were successfully identified. The inhibitory effect of the purified peptides from A. lecanora on NO production by lipopolysaccharide (LPS)-stimulated RAW 264.7 cells was investigated. The three identified bioactive peptides, namely LREMLSTMCTARGA, AVGPAGPRG and VAPAWGPWPKG, exhibited the highest NO-inhibitory activity with values of 76.3, 66.6 and 69.9%, respectively. These results revealed that A. lecanora could be used as an economical protein source for the production of high-value bioactive peptides with potent anti-inflammatory activity using RAW 264.7 cell lines as model. These peptides may be useful ingredients in food and pharmaceutical applications.
Research Interests:
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... 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 applications in the functional foods industries.
Research Interests:
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... 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 IC 50 were 1.4 and 0.2 µM, respectively.
Research Interests:
In recent years, food protein-derived hydrolysates have received considerable attention because of their numerous health benefits. Amongst the hydrolysates, those with anti-hypertensive and anti-oxidative activities are receiving special... more
In recent years, food protein-derived hydrolysates have received considerable attention
because of their numerous health benefits. Amongst the hydrolysates, those with anti-hypertensive
and anti-oxidative activities are receiving special attention as both activities can play significant
roles in preventing cardiovascular diseases. The present study investigated the angiotensin-I
converting enzyme (ACE) inhibitory and anti-oxidative activities of Actinopyga lecanora (A. lecanora)
hydrolysates, which had been prepared by alcalase, papain, bromelain, flavourzyme, pepsin,
and trypsin under their optimum conditions. The alcalase hydrolysate showed the highest
ACE inhibitory activity (69.8%) after 8 h of hydrolysis while the highest anti-oxidative activities
measured by 2,2-diphenyl 1-1-picrylhydrazyl radical scavenging (DPPH) (56.00%) and ferrous
ion-chelating (FIC) (59.00%) methods were exhibited after 24 h and 8 h of hydrolysis, respectively.
The ACE-inhibitory and anti-oxidative activities displayed dose-dependent trends, and increased
with increasing protein hydrolysate concentrations. Moreover, strong positive correlations between
angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidative activities were also observed.
This study indicates that A. lecanora hydrolysate can be exploited as a source of functional food
owing to its anti-oxidant as well as anti-hypertension functions.
because of their numerous health benefits. Amongst the hydrolysates, those with anti-hypertensive
and anti-oxidative activities are receiving special attention as both activities can play significant
roles in preventing cardiovascular diseases. The present study investigated the angiotensin-I
converting enzyme (ACE) inhibitory and anti-oxidative activities of Actinopyga lecanora (A. lecanora)
hydrolysates, which had been prepared by alcalase, papain, bromelain, flavourzyme, pepsin,
and trypsin under their optimum conditions. The alcalase hydrolysate showed the highest
ACE inhibitory activity (69.8%) after 8 h of hydrolysis while the highest anti-oxidative activities
measured by 2,2-diphenyl 1-1-picrylhydrazyl radical scavenging (DPPH) (56.00%) and ferrous
ion-chelating (FIC) (59.00%) methods were exhibited after 24 h and 8 h of hydrolysis, respectively.
The ACE-inhibitory and anti-oxidative activities displayed dose-dependent trends, and increased
with increasing protein hydrolysate concentrations. Moreover, strong positive correlations between
angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidative activities were also observed.
This study indicates that A. lecanora hydrolysate can be exploited as a source of functional food
owing to its anti-oxidant as well as anti-hypertension functions.
Research Interests:
Stichopus horrens is the most popular species of sea cucumber due to strong beliefs of its numerous medicinal properties. In this study, ACE-inhibitory peptides of S. horrens generated through enzymatic hydrolysis using Alcalase were... more
Stichopus horrens is the most popular species of sea cucumber due to strong beliefs of its
numerous medicinal properties. In this study, ACE-inhibitory peptides of S. horrens generated
through enzymatic hydrolysis using Alcalase were isolated. Three peptides EVSQGRP,
CRQNTLGHNTQTSIAQ and VSRHFASYAN were found to exhibit high inhibition potency with
IC50 values of 0.05, 0.08 and 0.21mM, respectively. It was found that the EVSQGRP,VSRHFASYAN
and SAAVGSP exhibiting mixed inhibition patterns were susceptible to degradation by ACE
as well, suggesting that themixed-mode inhibition could be a result of new generated peptide
fragments while CRQNTLGHNTQTSIAQ inhibited ACE in a non-competitive manner. Invivo
ACE inhibition studies showed that 400mg/kg of Alcalase-generated proteolysate stabilized
the blood pressure in normotensive rats. These results suggest that the hydrolysed protein
components of S. horrens possess bioactive peptides that can be exploited as functional food
ingredients against hypertension.
numerous medicinal properties. In this study, ACE-inhibitory peptides of S. horrens generated
through enzymatic hydrolysis using Alcalase were isolated. Three peptides EVSQGRP,
CRQNTLGHNTQTSIAQ and VSRHFASYAN were found to exhibit high inhibition potency with
IC50 values of 0.05, 0.08 and 0.21mM, respectively. It was found that the EVSQGRP,VSRHFASYAN
and SAAVGSP exhibiting mixed inhibition patterns were susceptible to degradation by ACE
as well, suggesting that themixed-mode inhibition could be a result of new generated peptide
fragments while CRQNTLGHNTQTSIAQ inhibited ACE in a non-competitive manner. Invivo
ACE inhibition studies showed that 400mg/kg of Alcalase-generated proteolysate stabilized
the blood pressure in normotensive rats. These results suggest that the hydrolysed protein
components of S. horrens possess bioactive peptides that can be exploited as functional food
ingredients against hypertension.
Research Interests:
This study was aimed to generate a valuable protein hydrolysate and bioactive peptides with strong ACE-inhibitory activity in vitro and in vivo from palm kernel cake (PKC) protein. PKC protein was independently hydrolyzed by seven... more
This study was aimed to generate a valuable protein hydrolysate and bioactive peptides with strong ACE-inhibitory activity in vitro and in vivo from palm kernel cake (PKC) protein. PKC protein was independently hydrolyzed by seven different proteases to produce PKC protein hydrolysates. Among those investigated, papain-produced hydrolysate revealed the highest ACE-inhibitory activity (70.9%). When normotensive rats induced with hypertension were fed the hydrolysate at a dose of 75 mg/kg body weight, their blood pressures stabilized considerably. Fractionation of the protein hydrolysate using RP-HPLC revealed a direct relationship between hydrophobicity and ACE-inhibitory activity. The fractions with relatively higher ACE-inhibitory activity were further fractionated by isoelectric focusing, out of which fractions having neutral and basic charges showing higher ACE-inhibitory activities (77% and 75%, respectively). Nine peptide sequences were identified by Q-TOF mass spectrometry, and their respective ACE-inhibitory activities evaluated. The peptide sequences YLLLK, YGIKVGYAIP, and LPWRPATNVF showed ACE-inhibitory activities of 100%; however, the best IC50 values were observed for YGIKVGYAIP, GIFE and LPWRPATNVF at 1 μM, 3 μM and 20 μM, respectively
Research Interests:
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,... 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.
Research Interests:
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... 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 high-performance 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.