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Nazamid Saari - One of the best experts on this subject based on the ideXlab platform.
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generation fractionation and characterization of iron chelating protein Hydrolysate from palm kernel cake proteins
Journal of Food Science, 2016Co-Authors: Mohammad Zarei, Azizah Abdulhamid, Rahele Ghanbari, Naser Tajabadi, Fatimah Abu Bakar, Nazamid SaariAbstract: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.
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angiotensin i converting enzyme ace inhibitory and anti oxidant activities of sea cucumber actinopyga lecanora Hydrolysates
International Journal of Molecular Sciences, 2015Co-Authors: Raheleh Ghanbari, Afshin Ebrahimpour, Mohammad Zarei, Azizah Abdulhamid, Amin Ismail, Nazamid SaariAbstract: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.
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actinopyga lecanora Hydrolysates as natural antibacterial agents
International Journal of Molecular Sciences, 2012Co-Authors: Raheleh Ghanbari, Afshin Ebrahimpour, Azizah Abdulhamid, Amin Ismail, Nazamid SaariAbstract:Actinopyga lecanora, a type of sea cucumber commonly known as stone fish with relatively high protein content, was explored as raw material for bioactive peptides production. Six proteolytic enzymes, namely alcalase, papain, pepsin, trypsin, bromelain and flavourzyme were used to hydrolyze A. lecanora at different times and their respective degrees of hydrolysis (DH) were calculated. Subsequently, antibacterial activity of the A. lecanora Hydrolysates, against some common pathogenic Gram positive bacteria (Bacillus subtilis and Staphylococcus aureus) and Gram negative bacteria (Escherichia coli, Pseudomonas aeruginosa, and Pseudomonas sp.) were evaluated. Papain hydrolysis showed the highest DH value (89.44%), followed by alcalase hydrolysis (83.35%). Bromelain Hydrolysate after one and seven hours of hydrolysis exhibited the highest antibacterial activities against Pseudomonas sp., P. aeruginosa and E. coli at 51.85%, 30.07% and 30.45%, respectively compared to the other Hydrolysates. Protein Hydrolysate generated by papain after 8 h hydrolysis showed maximum antibacterial activity against S. aureus at 20.19%. The potent Hydrolysates were further fractionated using RP-HPLC and antibacterial activity of the collected fractions from each Hydrolysate were evaluated, wherein among them only three fractions from the bromelain Hydrolysates exhibited inhibitory activities against Pseudomonas sp., P. aeruginosa and E. coli at 24%, 25.5% and 27.1%, respectively and one fraction of papain Hydrolysate showed antibacterial activity of 33.1% against S. aureus. The evaluation of the relationship between DH and antibacterial activities of papain and bromelain Hydrolysates revealed a meaningful correlation of four and six order functions.
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enzyme Hydrolysates from stichopus horrens as a new source for angiotensin converting enzyme inhibitory peptides
Evidence-based Complementary and Alternative Medicine, 2012Co-Authors: Bita Forghani, Afshin Ebrahimpour, Jamilah Bakar, Azizah Abdul Hamid, Zaiton Hassan, Nazamid SaariAbstract:Stichopus horrens flesh was explored as a potential source for generating peptides with angiotensin-converting enzyme (ACE) inhibitory capacity using 6 proteases, namely alcalase, flavourzyme, trypsin, papain, bromelain, and protamex. Degree of hydrolysis (DH) and peptide profiling (SDS-PAGE) of Stichopus horrens Hydrolysates (SHHs) was also assessed. Alcalase Hydrolysate showed the highest DH value (39.8%) followed by flavourzyme Hydrolysate (32.7%). Overall, alcalase Hydrolysate exhibited the highest ACE inhibitory activity (IC50 value of 0.41 mg/mL) followed by flavourzyme Hydrolysate (IC50 value of 2.24 mg/mL), trypsin Hydrolysate (IC50 value of 2.28 mg/mL), papain Hydrolysate (IC50 value of 2.48 mg/mL), bromelain Hydrolysate (IC50 value of 4.21 mg/mL), and protamex Hydrolysate (IC50 value of 6.38 mg/mL). The SDS-PAGE results showed that alcalase Hydrolysate represented a unique pattern compared to others, which yielded potent ACE inhibitory peptides with molecular weight distribution lower than 20 kDa. The evaluation of the relationship between DH and IC50 values of alcalase and flavourzyme Hydrolysates revealed that the trend between those parameters was related to the type of the protease used. We concluded that the tested SHHs would be used as a potential source of functional ACE inhibitory peptides for physiological benefits.
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production of defatted palm kernel cake protein Hydrolysate as a valuable source of natural antioxidants
International Journal of Molecular Sciences, 2012Co-Authors: Mohammad Zarei, Afshin Ebrahimpour, Azizah Abdulhamid, Farooq Anwar, Nazamid SaariAbstract: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.
Mohammad Zarei - One of the best experts on this subject based on the ideXlab platform.
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generation fractionation and characterization of iron chelating protein Hydrolysate from palm kernel cake proteins
Journal of Food Science, 2016Co-Authors: Mohammad Zarei, Azizah Abdulhamid, Rahele Ghanbari, Naser Tajabadi, Fatimah Abu Bakar, Nazamid SaariAbstract: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.
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angiotensin i converting enzyme ace inhibitory and anti oxidant activities of sea cucumber actinopyga lecanora Hydrolysates
International Journal of Molecular Sciences, 2015Co-Authors: Raheleh Ghanbari, Afshin Ebrahimpour, Mohammad Zarei, Azizah Abdulhamid, Amin Ismail, Nazamid SaariAbstract: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.
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production of defatted palm kernel cake protein Hydrolysate as a valuable source of natural antioxidants
International Journal of Molecular Sciences, 2012Co-Authors: Mohammad Zarei, Afshin Ebrahimpour, Azizah Abdulhamid, Farooq Anwar, Nazamid SaariAbstract: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.
Karl B Andree - One of the best experts on this subject based on the ideXlab platform.
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dietary aquaculture by product Hydrolysates impact on the transcriptomic response of the intestinal mucosa of european seabass dicentrarchus labrax fed low fish meal diets
BMC Genomics, 2018Co-Authors: Alexandre Leduc, Enric Gisbert, Celine Zatylnygaudin, Marie Robert, Erwan Corre, Gildas Le Corguille, Helene Castel, Antoine Lefevrescelles, Vincent Fournier, Karl B AndreeAbstract:Aquaculture production is expected to double by 2030, and demands for aquafeeds and raw materials are expected to increase accordingly. Sustainable growth of aquaculture will require the development of highly nutritive and functional raw materials to efficiently replace fish meal. Enzymatic hydrolysis of marine and aquaculture raw materials could bring new functionalities to finished products. The aim of this study was to determine the zootechnical and transcriptomic performances of protein Hydrolysates of different origins (tilapia, shrimp, and a combination of the two) in European seabass (Dicentrarchux labrax) fed a low fish meal diet (5%), for 65 days. Results were compared to a positive control fed with 20% of fish meal. Growth performances, anterior intestine histological organization and transcriptomic responses were monitored and analyzed. Dietary inclusion of protein Hydrolysates in the low fish meal diet restored similar growth performances to those of the positive control. Inclusion of dietary shrimp Hydrolysate resulted in larger villi and more goblet cells, even better than the positive control. Transcriptomic analysis of the anterior intestine showed that dietary Hydrolysate inclusion restored a pattern of intestinal gene expression very close to the pattern of the positive control. However, as compared to the low fish meal diet and depending on their origin, the different Hydrolysates did not modulate metabolic pathways in the same way. Dietary shrimp Hydrolysate inclusion modulated more metabolic pathways related to immunity, while nutritional metabolism was more impacted by dietary tilapia Hydrolysate. Interestingly, the combination of the two Hydrolysates enhanced the benefits of Hydrolysate inclusion in diets: more genes and metabolic pathways were regulated by the combined Hydrolysates than by each Hydrolysate tested independently. Protein Hydrolysates manufactured from aquaculture by-products are promising candidates to help replace fish meal in aquaculture feeds without disrupting animal metabolism and performances.
Richard J Fitzgerald - One of the best experts on this subject based on the ideXlab platform.
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In vitro α-glucosidase, angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory properties of brewers' spent grain protein Hydrolysates
Food Research International, 2014Co-Authors: Alan Connolly, Charles O. Piggott, Richard J FitzgeraldAbstract:Abstract The in vitro α-glucosidase, α-amylase, dipeptidyl peptidase IV (DPP-IV) and angiotensin converting enzyme (ACE) inhibitory activities of pale brewers' spent grain protein enriched isolate (BSG-PI) Hydrolysates were studied. Eleven commercially available enzyme preparations derived from papaya, porcine pancreas, Aspergillus oryzae and Bacillus licheniformis were used to generate the Hydrolysates. The Hydrolysates had degree hydrolysis (DH) values ranging from 1.15 to 14.67% and the DH values obtained correlated well with Hydrolysate molecular mass distribution profiles. Reverse-phase HPLC analysis of the BSG-PI and its Hydrolysates demonstrated considerable variation in peptide composition. While tryptic digests of BSG-PI resulted in the greatest α-glucosidase inhibitory activity, no significant change in α-amylase inhibition was observed with the Hydrolysates. Digestion with Corolase PP resulted in the highest DPP-IV inhibition (75 ± 3.06% at 3.5 mg mL − 1 ) while the Prolyve 1000 Hydrolysate displayed highest ACE inhibition (89.25 ± 2.46% at 1 mg mL − 1 ). The results obtained highlight the potential role of the BSG-PI Hydrolysates as functional food ingredients in the management of type II diabetes and hypertension.
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dipeptidyl peptidase iv inhibitory and antioxidative properties of milk protein derived dipeptides and Hydrolysates
Peptides, 2013Co-Authors: Alice B Nongonierma, Richard J FitzgeraldAbstract:Abstract Selected synthetic dipeptides and milk protein Hydrolysates were evaluated for their dipeptidyl peptidase IV (DPP-IV) inhibitory properties, and their superoxide (SO) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activities. DPP-IV inhibition was seen with eight out of the twelve dipeptides and 5 of the twelve Hydrolysates studied. Trp-Val inhibited DPP-IV, however, inhibition was not observed with the reverse peptide Val-Trp. The most potent Hydrolysate inhibitors were generated from casein (CasH2) and lactoferrin (LFH1). Two Trp containing dipeptides, Trp-Val and Val-Trp, and three lactoferrin Hydrolysates scavenged DPPH. The dipeptides had higher SO EC50 values compared to the milk protein Hydrolysates (arising from three lactoferrin and one whey protein Hydrolysates). Higher molecular mass fractions of the milk protein Hydrolysates were associated with the SO scavenging activity. Trp-Val and one lactoferrin Hydrolysate (LFH1) were multifunctional displaying both DPP-IV inhibitory and antioxidant (SO and DPPH scavenging) activities. These compounds may have potential as dietary ingredients in the management of type 2 diabetes by virtue of their ability to scavenge reactive oxygen species and to extend the half-life of incretin molecules.
T. Jyothirmayi - One of the best experts on this subject based on the ideXlab platform.
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antiproliferative ace inhibitory and functional properties of protein Hydrolysates from rohu labeo rohita roe egg prepared by gastrointestinal proteases
Journal of Food Science and Technology-mysore, 2015Co-Authors: Meram Chalamaiah, T. Jyothirmayi, Prakash V Diwan, Dinesh B KumarAbstract:Previously, we have reported the chemical composition, molecular mass distribution and antioxidant activity of rohu roe protein Hydrolysates. In the current study, antiproliferative, angiotensin-converting enzyme (ACE)-inhibitory activities and functional properties of protein Hydrolysates from rohu (Labeo rohita) roe proteins, prepared by gastrointestinal proteases (pepsin and trypsin), were investigated. Antiproliferative activity was evaluated against human colon cancer cell line Caco-2. The results showed that the pepsin Hydrolysate possessed dose dependent inhibitory effect on Caco-2 cell line. Pepsin and trypsin Hydrolysates displayed ACE-inhibitory activity in vitro. The ACE-inhibitory activity of the Hydrolysate generated by pepsin (47 ± 1.7 %, at 1 mg/ml) is higher than that obtained by trypsin (36 ± 3.2 %). Additionally, the undigested rohu roe proteins and its Hydrolysates exhibited functional properties. Solubilities of the Hydrolysates were above 81 ± 9.2 % at all pH values tested. Pepsin and trypsin Hydrolysates showed good foaming capacity (45-211 %) and emulsification activity (4-29 m(2)/g). The foaming abilities and emulsifying activity index (EAI) were affected by pH. The results suggest that protein Hydrolysates from rohu roe could be useful in food industry for various applications.
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protein Hydrolysates from meriga cirrhinus mrigala egg and evaluation of their functional properties
Food Chemistry, 2010Co-Authors: Meram Chalamaiah, Narsing G Rao, D G Rao, T. JyothirmayiAbstract:Protein Hydrolysates from underutilised meriga (Cirrhinus mrigala) fish egg were prepared by using commercial Alcalase and papain enzymes. The degree of hydrolysis was 62% for Alcalase and 17.1% for papain, after 90 min digestion at 50–55 and 60–65 °C, respectively. The protein content of Alcalase-produced Hydrolysate was higher (85%) than that of papain Hydrolysate (70%) (p < 0.05). Hydrolysis by both enzymes increased protein solubility of fish egg protein Hydrolysates to above 72.4% over a wide pH range (2–12). Results showed that the Hydrolysates had good fat absorption capacity (0.9 and 1.0 g/g sample), foam capacity (70% and 25%) and emulsifying capacity (4.25 and 5.98 ml/g Hydrolysate), respectively for Alcalase and papain protein Hydrolysates. Gel filtration chromatograms and SDS–PAGE analysis indicated the distribution of smaller peptides. These results suggested that fish egg protein Hydrolysates could be useful in the food industry.
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protein Hydrolysates from meriga cirrhinus mrigala egg and evaluation of their functional properties
Food Chemistry, 2010Co-Authors: Meram Chalamaiah, T. JyothirmayiAbstract:Protein Hydrolysates from underutilised meriga (Cirrhinus mrigala) fish egg were prepared by using commercial Alcalase and papain enzymes. The degree of hydrolysis was 62% for Alcalase and 17.1% for papain, after 90 min digestion at 50–55 and 60–65 °C, respectively. The protein content of Alcalase-produced Hydrolysate was higher (85%) than that of papain Hydrolysate (70%) (p < 0.05). Hydrolysis by both enzymes increased protein solubility of fish egg protein Hydrolysates to above 72.4% over a wide pH range (2–12). Results showed that the Hydrolysates had good fat absorption capacity (0.9 and 1.0 g/g sample), foam capacity (70% and 25%) and emulsifying capacity (4.25 and 5.98 ml/g Hydrolysate), respectively for Alcalase and papain protein Hydrolysates. Gel filtration chromatograms and SDS–PAGE analysis indicated the distribution of smaller peptides. These results suggested that fish egg protein Hydrolysates could be useful in the food industry.
