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Article: Thermal gelation of oat globulin
Title | Thermal gelation of oat globulin |
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Authors | |
Issue Date | 1988 |
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, 1988, v. 36 n. 2, p. 275-280 How to Cite? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/178375 |
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 | Khanzada, G | 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 | 1988 | en_US |
dc.identifier.citation | Journal Of Agricultural And Food Chemistry, 1988, v. 36 n. 2, p. 275-280 | en_US |
dc.identifier.issn | 0021-8561 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178375 | - |
dc.description.abstract | The 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.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 | Thermal gelation of 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-s2.0-0001215867 | en_US |
dc.identifier.volume | 36 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.spage | 275 | en_US |
dc.identifier.epage | 280 | en_US |
dc.identifier.isi | WOS:A1988M668500009 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_US |
dc.identifier.scopusauthorid | Khanzada, G=6508270535 | en_US |
dc.identifier.scopusauthorid | Harwalkar, VR=35605979700 | en_US |
dc.identifier.issnl | 0021-8561 | - |