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Article: Modulation of the thermal stability of β-lactoglobulin by transglutaminase treatment

TitleModulation of the thermal stability of β-lactoglobulin by transglutaminase treatment
Authors
KeywordsΒ-Lactoglobulin
Cross-Linking
Thermal Stability
Transglutaminase
Issue Date2007
PublisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00217/index.htm
Citation
European Food Research And Technology, 2007, v. 225 n. 5-6, p. 649-652 How to Cite?
AbstractThe influence of microbial transglutaminase (MTGase) treatment in the presence and absence of dithiothreitol (DTT) on the thermal stability of β-lactoglobulin (β-LG) was investigated using size-exclusion chromatography (SEC) combined with on-line multiangle laser light scattering (MALLS) and UV detection. SEC-MALLS-UV analyses showed that moderate MTGase treatment (up to 6 or 9 h) led to the decline in thermal stability of β-LG, while excess treatment (e.g. 23 h) resulted in remarkable increase, irrespective of whether the reducing agent DTT was present or not. The modulation in thermal stability may be attributed to the partial unfolding of protein molecules and the subsequent re-arrangement of conformation. © 2006 Springer-Verlag.
Persistent Identifierhttp://hdl.handle.net/10722/179010
ISSN
2015 Impact Factor: 1.433
2015 SCImago Journal Rankings: 0.726
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTang, CHen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:51:24Z-
dc.date.available2012-12-19T09:51:24Z-
dc.date.issued2007en_US
dc.identifier.citationEuropean Food Research And Technology, 2007, v. 225 n. 5-6, p. 649-652en_US
dc.identifier.issn1438-2377en_US
dc.identifier.urihttp://hdl.handle.net/10722/179010-
dc.description.abstractThe influence of microbial transglutaminase (MTGase) treatment in the presence and absence of dithiothreitol (DTT) on the thermal stability of β-lactoglobulin (β-LG) was investigated using size-exclusion chromatography (SEC) combined with on-line multiangle laser light scattering (MALLS) and UV detection. SEC-MALLS-UV analyses showed that moderate MTGase treatment (up to 6 or 9 h) led to the decline in thermal stability of β-LG, while excess treatment (e.g. 23 h) resulted in remarkable increase, irrespective of whether the reducing agent DTT was present or not. The modulation in thermal stability may be attributed to the partial unfolding of protein molecules and the subsequent re-arrangement of conformation. © 2006 Springer-Verlag.en_US
dc.languageengen_US
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00217/index.htmen_US
dc.relation.ispartofEuropean Food Research and Technologyen_US
dc.subjectΒ-Lactoglobulinen_US
dc.subjectCross-Linkingen_US
dc.subjectThermal Stabilityen_US
dc.subjectTransglutaminaseen_US
dc.titleModulation of the thermal stability of β-lactoglobulin by transglutaminase treatmenten_US
dc.typeArticleen_US
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_US
dc.identifier.authorityMa, CY=rp00759en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s00217-006-0460-4en_US
dc.identifier.scopuseid_2-s2.0-34547606993en_US
dc.identifier.hkuros145221-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34547606993&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume225en_US
dc.identifier.issue5-6en_US
dc.identifier.spage649en_US
dc.identifier.epage652en_US
dc.identifier.isiWOS:000248608400004-
dc.publisher.placeGermanyen_US
dc.identifier.scopusauthoridTang, CH=35197262700en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.citeulike5887240-

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