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

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TitleAcid modification of proteins from soymilk residue (okara)
AuthorsChan, WM
Ma, CY
KeywordsAcid modification
Deamidation
Okara
Protein functionality
Soymilk
Issue Date1999
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodres
CitationFood Research International, 1999, v. 32 n. 2, p. 119-127 [How to Cite?]
DOI: http://dx.doi.org/10.1016/S0963-9969(99)00064-2
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.
ISSN0963-9969
2011 Impact Factor: 3.15
2011 SCImago Journal Rankings: 0.107
DOIhttp://dx.doi.org/10.1016/S0963-9969(99)00064-2
ISI Accession Number IDWOS:000082564000005
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorChan, WM
dc.contributor.authorMa, CY
dc.date.accessioned2010-09-06T06:05:12Z
dc.date.available2010-09-06T06:05:12Z
dc.date.issued1999
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.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationFood Research International, 1999, v. 32 n. 2, p. 119-127 [How to Cite?]
DOI: http://dx.doi.org/10.1016/S0963-9969(99)00064-2
dc.identifier.doihttp://dx.doi.org/10.1016/S0963-9969(99)00064-2
dc.identifier.epage127
dc.identifier.hkuros45843
dc.identifier.isiWOS:000082564000005
dc.identifier.issn0963-9969
2011 Impact Factor: 3.15
2011 SCImago Journal Rankings: 0.107
dc.identifier.issue2
dc.identifier.openurl
dc.identifier.scopuseid_2-s2.0-0032850080
dc.identifier.spage119
dc.identifier.urihttp://hdl.handle.net/10722/68505
dc.identifier.volume32
dc.languageeng
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodres
dc.publisher.placeUnited Kingdom
dc.relation.ispartofFood Research International
dc.relation.referencesReferences in Scopus
dc.subjectAcid modification
dc.subjectDeamidation
dc.subjectOkara
dc.subjectProtein functionality
dc.subjectSoymilk
dc.titleAcid modification of proteins from soymilk residue (okara)
dc.typeArticle