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Article: Acid modification of proteins from soymilk residue (okara)

TitleAcid modification of proteins from soymilk residue (okara)
Authors
KeywordsAcid modification
Deamidation
Okara
Protein functionality
Soymilk
Issue Date1999
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodres
Citation
Food Research International, 1999, v. 32 n. 2, p. 119-127 How to Cite?
Abstract
Protein was extracted from soy residue (okara) at alkaline pH, and was modified by mild acid treatments. The degree of deamidation and peptide bond hydrolysis ranged from 10 to 70% and 6 to 15%, respectively. Size exclusion gel filtration chromatography revealed that there was a progressive degradation of the okara protein. Solubility was increased markedly by the modification, while other functional properties such as emulsifying and foaming properties Were also improved. The okara protein products have good essential amino acid profiles, and acid modification also increased the in vitro digestability and available lysine content of okara protein. The results indicate that changes in functional properties of okara protein by acid modification were attributed to changes in physicochemical properties such as decreases in molecular size, higher net titratable charge and surface hydrophobicity. The low solubility of okara protein makes it difficult to be incorporated into many food systems. Improved solubility and other functional properties by acid modification will enhance the utilization okara protein as food ingredient.
Persistent Identifierhttp://hdl.handle.net/10722/68505
ISSN
2013 Impact Factor: 3.050
2013 SCImago Journal Rankings: 1.528
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, WMen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:05:12Z-
dc.date.available2010-09-06T06:05:12Z-
dc.date.issued1999en_HK
dc.identifier.citationFood Research International, 1999, v. 32 n. 2, p. 119-127en_HK
dc.identifier.issn0963-9969en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68505-
dc.description.abstractProtein was extracted from soy residue (okara) at alkaline pH, and was modified by mild acid treatments. The degree of deamidation and peptide bond hydrolysis ranged from 10 to 70% and 6 to 15%, respectively. Size exclusion gel filtration chromatography revealed that there was a progressive degradation of the okara protein. Solubility was increased markedly by the modification, while other functional properties such as emulsifying and foaming properties Were also improved. The okara protein products have good essential amino acid profiles, and acid modification also increased the in vitro digestability and available lysine content of okara protein. The results indicate that changes in functional properties of okara protein by acid modification were attributed to changes in physicochemical properties such as decreases in molecular size, higher net titratable charge and surface hydrophobicity. The low solubility of okara protein makes it difficult to be incorporated into many food systems. Improved solubility and other functional properties by acid modification will enhance the utilization okara protein as food ingredient.en_HK
dc.languageengen_HK
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodresen_HK
dc.relation.ispartofFood Research Internationalen_HK
dc.subjectAcid modificationen_HK
dc.subjectDeamidationen_HK
dc.subjectOkaraen_HK
dc.subjectProtein functionalityen_HK
dc.subjectSoymilken_HK
dc.titleAcid modification of proteins from soymilk residue (okara)en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0963-9969&volume=32&spage=119&epage=127&date=1999&atitle=Acid+modification+of+proteins+from+soymilk++residue+(okara)en_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0963-9969(99)00064-2en_HK
dc.identifier.scopuseid_2-s2.0-0032850080en_HK
dc.identifier.hkuros45843en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032850080&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume32en_HK
dc.identifier.issue2en_HK
dc.identifier.spage119en_HK
dc.identifier.epage127en_HK
dc.identifier.isiWOS:000082564000005-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridChan, WM=55471369000en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

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