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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
2013 Impact Factor: 3.050
2013 SCImago Journal Rankings: 1.528
 
DOIhttp://dx.doi.org/10.1016/S0963-9969(99)00064-2
 
ISI Accession Number IDWOS:000082564000005
 
ReferencesReferences in Scopus
 
DC FieldValue
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
2013 Impact Factor: 3.050
2013 SCImago Journal Rankings: 1.528
 
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
 
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