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Article: Modification of proteins from soymilk residue (okara) by trypsin
Title | Modification of proteins from soymilk residue (okara) by trypsin |
---|---|
Authors | |
Keywords | Okara Protein functionality Soymilk Trypsin hydrolysis |
Issue Date | 1999 |
Publisher | Wiley-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? |
Abstract | Okara 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 Identifier | http://hdl.handle.net/10722/68593 |
ISSN | 2023 Impact Factor: 3.2 2023 SCImago Journal Rankings: 0.783 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Chan, WM | en_HK |
dc.contributor.author | Ma, CY | en_HK |
dc.date.accessioned | 2010-09-06T06:05:58Z | - |
dc.date.available | 2010-09-06T06:05:58Z | - |
dc.date.issued | 1999 | en_HK |
dc.identifier.citation | Journal Of Food Science, 1999, v. 64 n. 5, p. 781-786 | en_HK |
dc.identifier.issn | 0022-1147 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/68593 | - |
dc.description.abstract | Okara 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.language | eng | en_HK |
dc.publisher | Wiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-1147 | en_HK |
dc.relation.ispartof | Journal of Food Science | en_HK |
dc.subject | Okara | en_HK |
dc.subject | Protein functionality | en_HK |
dc.subject | Soymilk | en_HK |
dc.subject | Trypsin hydrolysis | en_HK |
dc.title | Modification of proteins from soymilk residue (okara) by trypsin | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://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+trypsin | en_HK |
dc.identifier.email | Ma, CY: macy@hkucc.hku.hk | en_HK |
dc.identifier.authority | Ma, CY=rp00759 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.scopus | eid_2-s2.0-0032700224 | en_HK |
dc.identifier.hkuros | 53358 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0032700224&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 64 | en_HK |
dc.identifier.issue | 5 | en_HK |
dc.identifier.spage | 781 | en_HK |
dc.identifier.epage | 786 | en_HK |
dc.identifier.isi | WOS:000083640700007 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Chan, WM=55471369000 | en_HK |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_HK |
dc.identifier.issnl | 0022-1147 | - |