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Article: Physicochemical properties of alkali-treated oat globulin

TitlePhysicochemical properties of alkali-treated oat globulin
Authors
Issue Date1990
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 1990, v. 38 n. 8, p. 1707-1711 How to Cite?
AbstractOat globulin dispersions (10% w/v) were incubated at an initial pH of 9.8 at 25, 37, and 55°C over a period of 96 h. Turbidity increased at 25 and 37°C with the formation of insoluble aggregates and decreased at 55°C with little precipitation. The free SH content decreased progressively with time, while the surface hydrophobicity was increased at 25°C and decreased at 37°C. Differential scanning calorimetry showed progressive increases in denaturation temperature and decreases in width at half-peak height. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated formation of soluble aggregates at 55°C and degradation of oat globulin polypeptides at 25 and 37°C, possibly due to proteolysis by protease(s) coextracted with the protein. No significant racemization of amino acids was observed in the alkali-treated protein.
Persistent Identifierhttp://hdl.handle.net/10722/178822
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_US
dc.contributor.authorHarwalkar, VRen_US
dc.contributor.authorPaquet, Aen_US
dc.date.accessioned2012-12-19T09:49:57Z-
dc.date.available2012-12-19T09:49:57Z-
dc.date.issued1990en_US
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 1990, v. 38 n. 8, p. 1707-1711en_US
dc.identifier.issn0021-8561en_US
dc.identifier.urihttp://hdl.handle.net/10722/178822-
dc.description.abstractOat globulin dispersions (10% w/v) were incubated at an initial pH of 9.8 at 25, 37, and 55°C over a period of 96 h. Turbidity increased at 25 and 37°C with the formation of insoluble aggregates and decreased at 55°C with little precipitation. The free SH content decreased progressively with time, while the surface hydrophobicity was increased at 25°C and decreased at 37°C. Differential scanning calorimetry showed progressive increases in denaturation temperature and decreases in width at half-peak height. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated formation of soluble aggregates at 55°C and degradation of oat globulin polypeptides at 25 and 37°C, possibly due to proteolysis by protease(s) coextracted with the protein. No significant racemization of amino acids was observed in the alkali-treated protein.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.titlePhysicochemical properties of alkali-treated 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-s2.0-0342431555en_US
dc.identifier.volume38en_US
dc.identifier.issue8en_US
dc.identifier.spage1707en_US
dc.identifier.epage1711en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridHarwalkar, VR=35605979700en_US
dc.identifier.scopusauthoridPaquet, A=7003782027en_US

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