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Article: Modification of proteins from soymilk residue (okara) by trypsin

TitleModification of proteins from soymilk residue (okara) by trypsin
Authors
Chan, WMMa, CY
KeywordsOkara
Protein functionality
Soymilk
Trypsin hydrolysis
Issue Date1999
PublisherWiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-1147
Citation
Journal Of Food Science, 1999, v. 64 n. 5, p. 781-786 How to Cite?
AbstractOkara protein isolates were hydrolyzed by trypsin to about 5% to 14%. Solubility was increased more than twofold by the modification, and water hydration capacity and emulsification activity index were also improved. The okara protein products had good essential amino acid profiles and the trypsin-hydrolysates also had increased in vitro digestibility and available lysine content. The low solubility of okara protein makes it difficult to incorporate it into many food systems. Okara protein hydrolysates, with improved solubility and other functional properties, could be used as a low-cost protein ingredient in processed foods.
Persistent Identifierhttp://hdl.handle.net/10722/68593
ISSN
0022-1147
2021 Impact Factor: 3.693
2020 SCImago Journal Rankings: 0.772
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorChan, WMen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:05:58Z-
dc.date.available2010-09-06T06:05:58Z-
dc.date.issued1999en_HK
dc.identifier.citationJournal Of Food Science, 1999, v. 64 n. 5, p. 781-786en_HK
dc.identifier.issn0022-1147en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68593-
dc.description.abstractOkara protein isolates were hydrolyzed by trypsin to about 5% to 14%. Solubility was increased more than twofold by the modification, and water hydration capacity and emulsification activity index were also improved. The okara protein products had good essential amino acid profiles and the trypsin-hydrolysates also had increased in vitro digestibility and available lysine content. The low solubility of okara protein makes it difficult to incorporate it into many food systems. Okara protein hydrolysates, with improved solubility and other functional properties, could be used as a low-cost protein ingredient in processed foods.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-1147en_HK
dc.relation.ispartofJournal of Food Scienceen_HK
dc.subjectOkaraen_HK
dc.subjectProtein functionalityen_HK
dc.subjectSoymilken_HK
dc.subjectTrypsin hydrolysisen_HK
dc.titleModification of proteins from soymilk residue (okara) by trypsinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-1147&volume=64&spage=781&epage=786&date=1999&atitle=Modification+of+proteins+from+soymilk+residue+(okara)+by+trypsinen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.scopuseid_2-s2.0-0032700224en_HK
dc.identifier.hkuros53358en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032700224&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume64en_HK
dc.identifier.issue5en_HK
dc.identifier.spage781en_HK
dc.identifier.epage786en_HK
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChan, WM=55471369000en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.issnl0022-1147-

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