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Article: Study of thermal properties and heat-induced denaturation and aggregation of soy proteins by modulated differential scanning calorimetry

TitleStudy of thermal properties and heat-induced denaturation and aggregation of soy proteins by modulated differential scanning calorimetry
Authors
KeywordsModulated differential scanning calorimetry (MDSC)
Soy proteins
Thermal property
Issue Date2007
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijbiomac
Citation
International Journal Of Biological Macromolecules, 2007, v. 40 n. 2, p. 96-104 How to Cite?
AbstractThe thermal properties and heat-induced denaturation and aggregation of soy protein isolates (SPI) were studied using modulated differential scanning calorimetry (MDSC). Reversible and non-reversible heat flow signals were separated from the total heat flow signals in the thermograms. In the non-reversible profiles, two major endothermic peaks (at around 100 and 220 °C, respectively) associated with the loss of residual water were identified. In the reversible profiles, an exothermic peak associated with thermal aggregation was observed. Soy proteins denatured to various extents by heat treatments showed different non-reversible and reversible heat flow patterns, especially the exothermic peak. The endothermic or exothermic transition characteristics in both non-reversible and reversible signals were affected by the thermal history of the samples. The enthalpy change of the exothermic (aggregation) peak increased almost linearly with increase in relative humidity (RH) in the range between 8 and 85%. In contrast, the onset temperature of the exotherm decreased progressively with increase in RH. These results suggest that the MDSC technique could be used to study thermal properties and heat-induced denaturation/aggregation of soy proteins at low moisture contents. Associated functional properties such as water holding and hydration property can also be evaluated. © 2006 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68604
ISSN
2015 Impact Factor: 3.138
2015 SCImago Journal Rankings: 0.815
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTang, CHen_HK
dc.contributor.authorChoi, SMen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:06:04Z-
dc.date.available2010-09-06T06:06:04Z-
dc.date.issued2007en_HK
dc.identifier.citationInternational Journal Of Biological Macromolecules, 2007, v. 40 n. 2, p. 96-104en_HK
dc.identifier.issn0141-8130en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68604-
dc.description.abstractThe thermal properties and heat-induced denaturation and aggregation of soy protein isolates (SPI) were studied using modulated differential scanning calorimetry (MDSC). Reversible and non-reversible heat flow signals were separated from the total heat flow signals in the thermograms. In the non-reversible profiles, two major endothermic peaks (at around 100 and 220 °C, respectively) associated with the loss of residual water were identified. In the reversible profiles, an exothermic peak associated with thermal aggregation was observed. Soy proteins denatured to various extents by heat treatments showed different non-reversible and reversible heat flow patterns, especially the exothermic peak. The endothermic or exothermic transition characteristics in both non-reversible and reversible signals were affected by the thermal history of the samples. The enthalpy change of the exothermic (aggregation) peak increased almost linearly with increase in relative humidity (RH) in the range between 8 and 85%. In contrast, the onset temperature of the exotherm decreased progressively with increase in RH. These results suggest that the MDSC technique could be used to study thermal properties and heat-induced denaturation/aggregation of soy proteins at low moisture contents. Associated functional properties such as water holding and hydration property can also be evaluated. © 2006 Elsevier B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijbiomacen_HK
dc.relation.ispartofInternational Journal of Biological Macromoleculesen_HK
dc.rightsInternational Journal of Biological Macromolecules. Copyright © Elsevier BV.en_HK
dc.subjectModulated differential scanning calorimetry (MDSC)en_HK
dc.subjectSoy proteinsen_HK
dc.subjectThermal propertyen_HK
dc.titleStudy of thermal properties and heat-induced denaturation and aggregation of soy proteins by modulated differential scanning calorimetryen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0141-8130&volume=40&spage=96&epage=104&date=2007&atitle=Study+of+thermal+properties+and+heat-induced+denaturation+and+aggregation+of+soy+proteins+by+modulated+differential+scanning+calorimetryen_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.ijbiomac.2006.06.013en_HK
dc.identifier.pmid16875727en_HK
dc.identifier.scopuseid_2-s2.0-33845893048en_HK
dc.identifier.hkuros128363en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845893048&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume40en_HK
dc.identifier.issue2en_HK
dc.identifier.spage96en_HK
dc.identifier.epage104en_HK
dc.identifier.isiWOS:000243674800005-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridTang, CH=35197262700en_HK
dc.identifier.scopusauthoridChoi, SM=8873744400en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.citeulike3813896-

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