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Article: Functional properties of oat proteins modified by acylation, trypsin hydrolysis or linoleate treatment

TitleFunctional properties of oat proteins modified by acylation, trypsin hydrolysis or linoleate treatment
Authors
Issue Date1987
Citation
Journal Of The American Oil Chemists' Society, 1987, v. 64 n. 12, p. 1726-1731 How to Cite?
AbstractProteins extracted from defatted oats were chemically modified by acylation (succinylation and acetylation), potassium linoleate treatment or partial hydrolysis with trypsin. Total essential amino acid content was slightly lowered by acetylation, but unaffected by succinylation. Gel filtration chromatography showed some dissociation of oat polypeptides by succinylation, while trypsin hydrolysis caused considerable breakdown of the protein. Solubility and emulsifying properties were significantly improved by all the modifications. Fat binding capacity was improved by acylation and linoleate treatment, while water hydration capacity and foaming properties were improved by trypsin and linoleate modifications. The gelling property was improved by acylation. When meat protein was substituted with oat protein in model wieners, there was a decrease in cook yield, cohesiveness and firmness. However, when compared to the unmodified oat protein, succinylation led to an improvement in performance in an emulsified meat system. © 1987 AOCS Press.
Persistent Identifierhttp://hdl.handle.net/10722/178462
ISSN
2015 Impact Factor: 1.505
2015 SCImago Journal Rankings: 0.676
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_US
dc.contributor.authorWood, DFen_US
dc.date.accessioned2012-12-19T09:47:50Z-
dc.date.available2012-12-19T09:47:50Z-
dc.date.issued1987en_US
dc.identifier.citationJournal Of The American Oil Chemists' Society, 1987, v. 64 n. 12, p. 1726-1731en_US
dc.identifier.issn0003-021Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/178462-
dc.description.abstractProteins extracted from defatted oats were chemically modified by acylation (succinylation and acetylation), potassium linoleate treatment or partial hydrolysis with trypsin. Total essential amino acid content was slightly lowered by acetylation, but unaffected by succinylation. Gel filtration chromatography showed some dissociation of oat polypeptides by succinylation, while trypsin hydrolysis caused considerable breakdown of the protein. Solubility and emulsifying properties were significantly improved by all the modifications. Fat binding capacity was improved by acylation and linoleate treatment, while water hydration capacity and foaming properties were improved by trypsin and linoleate modifications. The gelling property was improved by acylation. When meat protein was substituted with oat protein in model wieners, there was a decrease in cook yield, cohesiveness and firmness. However, when compared to the unmodified oat protein, succinylation led to an improvement in performance in an emulsified meat system. © 1987 AOCS Press.en_US
dc.languageengen_US
dc.relation.ispartofJournal of the American Oil Chemists' Societyen_US
dc.titleFunctional properties of oat proteins modified by acylation, trypsin hydrolysis or linoleate treatmenten_US
dc.typeArticleen_US
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_US
dc.identifier.authorityMa, CY=rp00759en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/BF02542510en_US
dc.identifier.scopuseid_2-s2.0-0023597146en_US
dc.identifier.volume64en_US
dc.identifier.issue12en_US
dc.identifier.spage1726en_US
dc.identifier.epage1731en_US
dc.identifier.isiWOS:A1987L502600016-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridWood, DF=16461601200en_US

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