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Article: Thermal gelation of oat globulin

TitleThermal gelation of oat globulin
Authors
Issue Date1988
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 1988, v. 36 n. 2, p. 275-280 How to Cite?
AbstractThe thermal gelation properties of oat globulin were studied under different conditions of temperature, protein concentration, pH, and ionic strength. Differential scanning calorimetry shows that oat globulin heated under conditions inducing gelation was not extensively denatured and exhibited highly cooperative transition characteristics. The chemical forces involved in gel formation were investigated by measuring the gel hardness under the influence of neutral salts, reducing agents, denaturants, and water-miscible solvent. Some fatty acid salts were effective in improving the gelling property of oat globulin near neutral pH.
Persistent Identifierhttp://hdl.handle.net/10722/178375
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_US
dc.contributor.authorKhanzada, Gen_US
dc.contributor.authorHarwalkar, VRen_US
dc.date.accessioned2012-12-19T09:47:20Z-
dc.date.available2012-12-19T09:47:20Z-
dc.date.issued1988en_US
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 1988, v. 36 n. 2, p. 275-280en_US
dc.identifier.issn0021-8561en_US
dc.identifier.urihttp://hdl.handle.net/10722/178375-
dc.description.abstractThe thermal gelation properties of oat globulin were studied under different conditions of temperature, protein concentration, pH, and ionic strength. Differential scanning calorimetry shows that oat globulin heated under conditions inducing gelation was not extensively denatured and exhibited highly cooperative transition characteristics. The chemical forces involved in gel formation were investigated by measuring the gel hardness under the influence of neutral salts, reducing agents, denaturants, and water-miscible solvent. Some fatty acid salts were effective in improving the gelling property of oat globulin near neutral pH.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_US
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_US
dc.titleThermal gelation of oat globulinen_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.scopuseid_2-s2.0-0001215867en_US
dc.identifier.volume36en_US
dc.identifier.issue2en_US
dc.identifier.spage275en_US
dc.identifier.epage280en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridKhanzada, G=6508270535en_US
dc.identifier.scopusauthoridHarwalkar, VR=35605979700en_US

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