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Article: Chemical characterization and functionality assessment of oat protein fractions

TitleChemical characterization and functionality assessment of oat protein fractions
Authors
Ma, CYHarwalkar, VR
Issue Date1984
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 1984, v. 32 n. 1, p. 144-149 How to Cite?
AbstractProtein fractions (albumins, globulins, prolamins, and glutelins) were prepared from oat seeds (variety Sentinel). Column chromatography on Sephacryl S-200 revealed that the four solubility fractions had unique polypeptide compositions and there was little cross contamination among the fractions. Isoelectric focusing on polyacrylamide gels resolved the fractions into a large number of bands covering a wide pH range. Differential scanning calorimetric studies showed that albumins and globulins had an endothermic peak at 87 and 110 °C, respectively, while prolamins and glutelins had no thermal response. Some functional properties of the solubility fractions were determined to assess the potential use of oat proteins as a food ingredient. Some fractions had high emulsifying, fat-binding, and water hydration capacities, and the albumins also had excellent foaming properties.
Persistent Identifierhttp://hdl.handle.net/10722/178376
ISSN
0021-8561
2021 Impact Factor: 5.895
2020 SCImago Journal Rankings: 1.203

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_US
dc.contributor.authorHarwalkar, VRen_US
dc.date.accessioned2012-12-19T09:47:20Z-
dc.date.available2012-12-19T09:47:20Z-
dc.date.issued1984en_US
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 1984, v. 32 n. 1, p. 144-149en_US
dc.identifier.issn0021-8561en_US
dc.identifier.urihttp://hdl.handle.net/10722/178376-
dc.description.abstractProtein fractions (albumins, globulins, prolamins, and glutelins) were prepared from oat seeds (variety Sentinel). Column chromatography on Sephacryl S-200 revealed that the four solubility fractions had unique polypeptide compositions and there was little cross contamination among the fractions. Isoelectric focusing on polyacrylamide gels resolved the fractions into a large number of bands covering a wide pH range. Differential scanning calorimetric studies showed that albumins and globulins had an endothermic peak at 87 and 110 °C, respectively, while prolamins and glutelins had no thermal response. Some functional properties of the solubility fractions were determined to assess the potential use of oat proteins as a food ingredient. Some fractions had high emulsifying, fat-binding, and water hydration capacities, and the albumins also had excellent foaming properties.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.titleChemical characterization and functionality assessment of oat protein fractionsen_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-s2.0-0001276169en_US
dc.identifier.volume32en_US
dc.identifier.issue1en_US
dc.identifier.spage144en_US
dc.identifier.epage149en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridHarwalkar, VR=35605979700en_US
dc.identifier.issnl0021-8561-

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