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Article: Chemical characterization and functionality assessment of oat protein fractions
Title | Chemical characterization and functionality assessment of oat protein fractions |
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Authors | |
Issue Date | 1984 |
Publisher | American 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? |
Abstract | Protein 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 Identifier | http://hdl.handle.net/10722/178376 |
ISSN | 2023 Impact Factor: 5.7 2023 SCImago Journal Rankings: 1.114 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Ma, CY | en_US |
dc.contributor.author | Harwalkar, VR | en_US |
dc.date.accessioned | 2012-12-19T09:47:20Z | - |
dc.date.available | 2012-12-19T09:47:20Z | - |
dc.date.issued | 1984 | en_US |
dc.identifier.citation | Journal Of Agricultural And Food Chemistry, 1984, v. 32 n. 1, p. 144-149 | en_US |
dc.identifier.issn | 0021-8561 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178376 | - |
dc.description.abstract | Protein 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.language | eng | en_US |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau | en_US |
dc.relation.ispartof | Journal of Agricultural and Food Chemistry | en_US |
dc.title | Chemical characterization and functionality assessment of oat protein fractions | en_US |
dc.type | Article | en_US |
dc.identifier.email | Ma, CY: macy@hkucc.hku.hk | en_US |
dc.identifier.authority | Ma, CY=rp00759 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.scopus | eid_2-s2.0-0001276169 | en_US |
dc.identifier.volume | 32 | en_US |
dc.identifier.issue | 1 | en_US |
dc.identifier.spage | 144 | en_US |
dc.identifier.epage | 149 | en_US |
dc.identifier.isi | WOS:A1984SA71200036 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_US |
dc.identifier.scopusauthorid | Harwalkar, VR=35605979700 | en_US |
dc.identifier.issnl | 0021-8561 | - |