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Article: Study of Thermal Aggregation of Oat Globulin by Laser Light Scattering

TitleStudy of Thermal Aggregation of Oat Globulin by Laser Light Scattering
Authors
KeywordsLaser light scattering
Oat globulin
Quasi-elastic light scattering
Thermal aggregation
Issue Date2004
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 2004, v. 52 n. 10, p. 3089-3096 How to Cite?
AbstractThe heat-induced aggregation of oat globulin was studied using size-exclusion chromatography (SEC) combined with on-line multiangle laser light scattering (MALLS) and quasi-elastic light scattering (QELS). The unheated oat globulin exists as a mixture of hexamer (> 95%), trimer, and dimer forms of hexamer. The molecular weight of the hexamer was estimated by MALLS to be 330 000, close to that deduced from the genomic cloned data of the acidic and basic polypeptides of oat globulin. From QELS measurements, it can be predicted that the hexamer exists as two annular trimeric rings, with a diameter of 11.8 nm, placed on top of each other, forming an oblate cylinder with a height of about 8.5 nm. Upon heating at 100 °C, the oat globulin hexamers and trimers were dissociated into monomers. The heat-denatured monomers, probably assuming an extended structure, were associated to form small aggregates, which were further aggregated to high molecular weight complexes. Upon further heating (60 min), the soluble aggregates were associated to form insoluble aggregates. Aggregation of oat globulin occurred at a much faster rate at 110 °C. The results indicate that the SEC-MALLS-QELS system is suitable for studying thermal aggregation of food proteins.
Persistent Identifierhttp://hdl.handle.net/10722/68451
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhao, Yen_HK
dc.contributor.authorMine, Yen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:04:44Z-
dc.date.available2010-09-06T06:04:44Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 2004, v. 52 n. 10, p. 3089-3096en_HK
dc.identifier.issn0021-8561en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68451-
dc.description.abstractThe heat-induced aggregation of oat globulin was studied using size-exclusion chromatography (SEC) combined with on-line multiangle laser light scattering (MALLS) and quasi-elastic light scattering (QELS). The unheated oat globulin exists as a mixture of hexamer (> 95%), trimer, and dimer forms of hexamer. The molecular weight of the hexamer was estimated by MALLS to be 330 000, close to that deduced from the genomic cloned data of the acidic and basic polypeptides of oat globulin. From QELS measurements, it can be predicted that the hexamer exists as two annular trimeric rings, with a diameter of 11.8 nm, placed on top of each other, forming an oblate cylinder with a height of about 8.5 nm. Upon heating at 100 °C, the oat globulin hexamers and trimers were dissociated into monomers. The heat-denatured monomers, probably assuming an extended structure, were associated to form small aggregates, which were further aggregated to high molecular weight complexes. Upon further heating (60 min), the soluble aggregates were associated to form insoluble aggregates. Aggregation of oat globulin occurred at a much faster rate at 110 °C. The results indicate that the SEC-MALLS-QELS system is suitable for studying thermal aggregation of food proteins.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_HK
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_HK
dc.subjectLaser light scatteringen_HK
dc.subjectOat globulinen_HK
dc.subjectQuasi-elastic light scatteringen_HK
dc.subjectThermal aggregationen_HK
dc.titleStudy of Thermal Aggregation of Oat Globulin by Laser Light Scatteringen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8561&volume=52&spage=3089&epage=3096&date=2004&atitle=Study+of+thermal+aggregation+of+oat+globulin+by+laser+light+scatteringen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jf030735yen_HK
dc.identifier.pmid15137858-
dc.identifier.scopuseid_2-s2.0-2442503747en_HK
dc.identifier.hkuros91782en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-2442503747&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume52en_HK
dc.identifier.issue10en_HK
dc.identifier.spage3089en_HK
dc.identifier.epage3096en_HK
dc.identifier.isiWOS:000221419500051-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZhao, Y=14059361400en_HK
dc.identifier.scopusauthoridMine, Y=7103350429en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

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