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Article: Thermal aggregation of globulin from an indigenous Chinese legume, Phaseolus angularis (red bean)

TitleThermal aggregation of globulin from an indigenous Chinese legume, Phaseolus angularis (red bean)
Authors
KeywordsGlobulin
Phaseolus angularis
Protein
Thermal aggregation
Issue Date2002
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchem
Citation
Food Chemistry, 2002, v. 79 n. 1, p. 93-103 How to Cite?
AbstractThe thermal aggregation behavior of red bean (Phaseolus angularis) globulin (RBG) was studied at ≈1% (w/v) protein concentration in 0.01 M phosphate buffer, pH 7.4. The percentage of protein precipitated was affected by heating temperature, heating time and salt concentration. The influences of several salts of the chaotropic series and protein structure-modifying agents on thermal coagulation of RBG were also investigated. The effects of chaotropic salts did not follow the lyotropic series of anions. Sodium dodecyl sulfate caused a more pronounced reduction in heat-induced aggregation of RBG than did dithiothreitol, while N-ethylmaleimide did not affect aggregation until after a long heating period. Differential scanning calorimetric (DSC) data showed that heat aggregation of RBG was preceded by thermal denaturation. SDS-PAGE showed that heating led to the disappearance of some protein bands, and the basic polypeptide of 11S globulin (legumin) was not found in the buffer-soluble aggregates. Heating caused increases of surface hydrophobicity, again suggesting protein unfolding prior to aggregate formation. The buffer-insoluble aggregates did not show any DSC response, indicating extensive denaturation, and had a lower surface hydrophobicity and higher disulfide content than the buffer-soluble aggregates. The data suggest that electrostatic and hydrophobic interactions may play an important role in thermal aggregation of RBG, with disulfide bonds playing a limited role. © 2002 Elsevier Science Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68717
ISSN
2015 Impact Factor: 4.052
2015 SCImago Journal Rankings: 1.620
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMeng, GTen_HK
dc.contributor.authorChing, KMen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:07:01Z-
dc.date.available2010-09-06T06:07:01Z-
dc.date.issued2002en_HK
dc.identifier.citationFood Chemistry, 2002, v. 79 n. 1, p. 93-103en_HK
dc.identifier.issn0308-8146en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68717-
dc.description.abstractThe thermal aggregation behavior of red bean (Phaseolus angularis) globulin (RBG) was studied at ≈1% (w/v) protein concentration in 0.01 M phosphate buffer, pH 7.4. The percentage of protein precipitated was affected by heating temperature, heating time and salt concentration. The influences of several salts of the chaotropic series and protein structure-modifying agents on thermal coagulation of RBG were also investigated. The effects of chaotropic salts did not follow the lyotropic series of anions. Sodium dodecyl sulfate caused a more pronounced reduction in heat-induced aggregation of RBG than did dithiothreitol, while N-ethylmaleimide did not affect aggregation until after a long heating period. Differential scanning calorimetric (DSC) data showed that heat aggregation of RBG was preceded by thermal denaturation. SDS-PAGE showed that heating led to the disappearance of some protein bands, and the basic polypeptide of 11S globulin (legumin) was not found in the buffer-soluble aggregates. Heating caused increases of surface hydrophobicity, again suggesting protein unfolding prior to aggregate formation. The buffer-insoluble aggregates did not show any DSC response, indicating extensive denaturation, and had a lower surface hydrophobicity and higher disulfide content than the buffer-soluble aggregates. The data suggest that electrostatic and hydrophobic interactions may play an important role in thermal aggregation of RBG, with disulfide bonds playing a limited role. © 2002 Elsevier Science Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchemen_HK
dc.relation.ispartofFood Chemistryen_HK
dc.rightsFood Chemistry. Copyright © Elsevier BV.en_HK
dc.subjectGlobulinen_HK
dc.subjectPhaseolus angularisen_HK
dc.subjectProteinen_HK
dc.subjectThermal aggregationen_HK
dc.titleThermal aggregation of globulin from an indigenous Chinese legume, Phaseolus angularis (red bean)en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0308-8146&volume=79&spage=93&epage=103&date=2002&atitle=Thermal+aggregation+of+globulin+from+an+Indigenous+Chinese+legume,+Phaseolus+angularis+(red+bean)en_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/S0308-8146(02)00184-Xen_HK
dc.identifier.scopuseid_2-s2.0-0036824063en_HK
dc.identifier.hkuros81521en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036824063&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume79en_HK
dc.identifier.issue1en_HK
dc.identifier.spage93en_HK
dc.identifier.epage103en_HK
dc.identifier.isiWOS:000178301900013-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridMeng, GT=13405928600en_HK
dc.identifier.scopusauthoridChing, KM=7005739215en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

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