Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/45053
DC FieldValueLanguage
dc.contributor.authorCheng, F.Y.en_US
dc.contributor.author林亮全zh_TW
dc.contributor.authorWan, T.C.en_US
dc.contributor.authorLiu, Y.T.en_US
dc.contributor.authorChen, C.M.en_US
dc.contributor.authorLin, L.C.en_US
dc.contributor.authorSakata, R.en_US
dc.date2009zh_TW
dc.date.accessioned2014-06-06T08:14:21Z-
dc.date.available2014-06-06T08:14:21Z-
dc.identifier.issn1344-3941zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/45053-
dc.description.abstractThis study aims to identify peptides with angiotensin-I converting enzyme (ACE) inhibitory activity in hydrolysate from chicken leg bone protein hydrolyzed with alcalase for 4 h (A4H). The hydrolysate has demonstrated potent in vitro ACE inhibitory activity, and has been shown to attenuate the development of hypertension and cardiovascular hypertrophy in spontaneously hypertensive rats (SHR). A4H is competitive for ACE and was separated using high-performance liquid chromatography (HPLC) with a gel filtration column (Superdex Peptide HR 10/30). The results show that A4H is a mixed non-competitive inhibitor. Eighteen fractions were detected after separation of A4H, and most of them showed ACE inhibitory activity. Five fractions with strong ACE inhibitory activities (above 50%) were labeled from A to E. In addition, there were 10 peptides, consisting of 5-10 amino acid residues that were identified from fraction D that exhibited the strongest ACE inhibitory activity. Three of the identified peptides corresponded to peptides derived from collagen type I and chicken muscular protein. It is revealed that A4H has several peptides that possess ACE inhibitory activities.en_US
dc.language.isoen_USzh_TW
dc.relationAnimal Science Journalen_US
dc.relation.ispartofseriesAnimal Science Journal, Volume 80, Issue 1, Page(s) 91-97.en_US
dc.relation.urihttp://dx.doi.org/10.1111/j.1740-0929.2008.00601.xen_US
dc.subjectanimal by-producten_US
dc.subjectantihypertensionen_US
dc.subjectchicken boneen_US
dc.subjecthydrolysisen_US
dc.subjectpeptidesen_US
dc.subjectspontaneously hypertensive-ratsen_US
dc.subjectantihypertensive activityen_US
dc.subjectblood-pressureen_US
dc.subjectframe proteinen_US
dc.subjectfood proteinsen_US
dc.subjectbreast muscleen_US
dc.subjectpurificationen_US
dc.titleDetermination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with alcalaseen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1111/j.1740-0929.2008.00601.xzh_TW
item.languageiso639-1en_US-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextno fulltext-
Appears in Collections:動物科學系
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