Publication:
Enzyme hydrolysates from stichopus horrens as a new source for angiotensin-converting enzyme inhibitory peptides

Simple item page
dc.Chemicals/CASbromelain, 37189-34-7, 9001-00-7; papain, 9001-73-4; subtilisin, 9014-01-1; trypsin, 9002-07-7
dc.citedby26
dc.contributor.affiliationsFaculty of Science and Technology
dc.contributor.affiliationsUniversiti Putra Malaysia (UPM)
dc.contributor.affiliationsUniversiti Sains Islam Malaysia (USIM)
dc.contributor.authorForghani B.en_US
dc.contributor.authorEbrahimpour A.en_US
dc.contributor.authorBakar J.en_US
dc.contributor.authorAbdul Hamid A.en_US
dc.contributor.authorHassan Z.en_US
dc.contributor.authorSaari N.en_US
dc.date.accessioned2024-05-29T02:04:09Z
dc.date.available2024-05-29T02:04:09Z
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 (IC 50 value of 0.41 mg/mL) followed by flavourzyme hydrolysate (IC 50 value of 2.24 mg/mL), trypsin hydrolysate (IC 50 value of 2.28 mg/mL), papain hydrolysate (IC 50 value of 2.48 mg/mL), bromelain hydrolysate (IC 50 value of 4.21 mg/mL), and protamex hydrolysate (IC 50 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 IC 50 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. � 2012 Bita Forghani et al.en_US
dc.description.natureFinalen_US
dc.identifier.ArtNo236384
dc.identifier.doi10.1155/2012/236384
dc.identifier.issn1741427X
dc.identifier.scopus2-s2.0-84866168953
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84866168953&doi=10.1155%2f2012%2f236384&partnerID=40&md5=d956269e71884ab079b05c7fd56bea6c
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/10284
dc.identifier.volume2012
dc.languageEnglish
dc.language.isoen_USen_US
dc.relation.ispartofOpen Accessen_US
dc.relation.ispartofEvidence-based Complementary and Alternative Medicine
dc.sourceScopus
dc.titleEnzyme hydrolysates from stichopus horrens as a new source for angiotensin-converting enzyme inhibitory peptidesen_US
dc.title.alternativeEvid.-Based Complement. Altern. Med.en_US
dc.typeArticleen_US
dspace.entity.typePublication

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Enzyme hydrolysates from stichopus horrens as a new source for angiotensin-converting enzyme inhibitory peptides.pdf
Size:
2.27 MB
Format:
Adobe Portable Document Format
Download

Collections

Scopus