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Article: Thermal properties of globulin from rice (Oryza sativa) seeds

TitleThermal properties of globulin from rice (Oryza sativa) seeds
Authors
KeywordsDifferential scanning calorimetry
Globulin
Oryza sativa
Protein denaturation
Issue Date2006
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodres
Citation
Food Research International, 2006, v. 39 n. 3, p. 257-264 How to Cite?
AbstractThe thermal properties of rice (Oryza sativa) seed globulin were studied by differential scanning calorimetry (DSC) under the influence of various medium conditions. The denaturation temperatures (T d) of crude and purified rice globulin were 97.6 and 98.5°C, respectively. Increasing salt concentration enhanced thermal stability of rice globulin. The effect of chaotropic anions on DSC characteristics of rice globulin followed the order of the lyotropic series indicating progressive decreases in both T d and enthalpy (ΔH). Extreme pHs and protein perturbants (sodium dodecyl sulfate at above 20 mM, dithiothreitol, urea and ethylene glycol) caused marked protein denaturation and loss of thermal stability. In contrast, N-ethylmaleimide and SDS at below 20 mM exerted a stabilizing effect on rice globulin. Pre-heat treatments led to partial unfolding of rice globulin, and the level of denaturation increased progressively with increasing heating time. © 2005 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68647
ISSN
2015 Impact Factor: 3.182
2015 SCImago Journal Rankings: 1.539
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorEllepola, SWen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:06:26Z-
dc.date.available2010-09-06T06:06:26Z-
dc.date.issued2006en_HK
dc.identifier.citationFood Research International, 2006, v. 39 n. 3, p. 257-264en_HK
dc.identifier.issn0963-9969en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68647-
dc.description.abstractThe thermal properties of rice (Oryza sativa) seed globulin were studied by differential scanning calorimetry (DSC) under the influence of various medium conditions. The denaturation temperatures (T d) of crude and purified rice globulin were 97.6 and 98.5°C, respectively. Increasing salt concentration enhanced thermal stability of rice globulin. The effect of chaotropic anions on DSC characteristics of rice globulin followed the order of the lyotropic series indicating progressive decreases in both T d and enthalpy (ΔH). Extreme pHs and protein perturbants (sodium dodecyl sulfate at above 20 mM, dithiothreitol, urea and ethylene glycol) caused marked protein denaturation and loss of thermal stability. In contrast, N-ethylmaleimide and SDS at below 20 mM exerted a stabilizing effect on rice globulin. Pre-heat treatments led to partial unfolding of rice globulin, and the level of denaturation increased progressively with increasing heating time. © 2005 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodresen_HK
dc.relation.ispartofFood Research Internationalen_HK
dc.subjectDifferential scanning calorimetryen_HK
dc.subjectGlobulinen_HK
dc.subjectOryza sativaen_HK
dc.subjectProtein denaturationen_HK
dc.titleThermal properties of globulin from rice (Oryza sativa) seedsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0963-9969&volume=39&spage=257&epage=264&date=2006&atitle=Thermal+properties+of+globulin+from+rice+(Oryza+sativa)+seedsen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.foodres.2005.07.015en_HK
dc.identifier.scopuseid_2-s2.0-28844481346en_HK
dc.identifier.hkuros115301en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-28844481346&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume39en_HK
dc.identifier.issue3en_HK
dc.identifier.spage257en_HK
dc.identifier.epage264en_HK
dc.identifier.isiWOS:000235649200001-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridEllepola, SW=9843111000en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

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