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Article: Physicochemical properties of alkali-treated oat globulin
Title | Physicochemical properties of alkali-treated oat globulin |
---|---|
Authors | |
Issue Date | 1990 |
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, 1990, v. 38 n. 8, p. 1707-1711 How to Cite? |
Abstract | Oat 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 Identifier | http://hdl.handle.net/10722/178822 |
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.contributor.author | Paquet, A | en_US |
dc.date.accessioned | 2012-12-19T09:49:57Z | - |
dc.date.available | 2012-12-19T09:49:57Z | - |
dc.date.issued | 1990 | en_US |
dc.identifier.citation | Journal Of Agricultural And Food Chemistry, 1990, v. 38 n. 8, p. 1707-1711 | en_US |
dc.identifier.issn | 0021-8561 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178822 | - |
dc.description.abstract | Oat 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.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 | Physicochemical properties of alkali-treated oat globulin | 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-s2.0-0342431555 | en_US |
dc.identifier.volume | 38 | en_US |
dc.identifier.issue | 8 | en_US |
dc.identifier.spage | 1707 | en_US |
dc.identifier.epage | 1711 | en_US |
dc.identifier.isi | WOS:A1990DV74700017 | - |
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.scopusauthorid | Paquet, A=7003782027 | en_US |
dc.identifier.issnl | 0021-8561 | - |