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Enzyme Hydrolysates from Stichopus horrens as a New Source for Angiotensin-Converting Enzyme Inhibitory Peptides

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dc.contributor.authorForghani, Ben_US
dc.contributor.authorEbrahimpour, Aen_US
dc.contributor.authorBakar, Jen_US
dc.contributor.authorHamid, AAen_US
dc.contributor.authorHassan, Zen_US
dc.contributor.authorSaari, Nen_US
dc.date.accessioned2024-05-29T03:25:47Z
dc.date.available2024-05-29T03:25:47Z
dc.date.issued2012
dc.description.abstractStichopus 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.
dc.identifier.doi10.1155/2012/236384
dc.identifier.issn1741-427X
dc.identifier.scopusWOS:000308198700001
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/12028
dc.languageEnglish
dc.language.isoen_US
dc.publisherHindawi Publishing Corporationen_US
dc.relation.ispartofEvidence-Based Complementary And Alternative Medicine
dc.sourceWeb Of Science (ISI)
dc.titleEnzyme Hydrolysates from Stichopus horrens as a New Source for Angiotensin-Converting Enzyme Inhibitory Peptides
dc.typeArticleen_US
dspace.entity.typePublication

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