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Article: Physicochemical and structural properties of oat globulin polymers formed by a microbial transglutaminase

TitlePhysicochemical and structural properties of oat globulin polymers formed by a microbial transglutaminase
Authors
KeywordsDSC
Flow properties
FTIR spectroscopy
Oat globulin
Protein polymerization
Structural properties
Transglutaminase
Issue Date2002
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 2002, v. 50 n. 9, p. 2660-2665 How to Cite?
AbstractOat globulin was polymerized by a microbial transglutaminase (TG), and some physicochemical and functional properties of polymers were studied. Reversed-phase HPLC revealed that the number of ε-(γ-glutamyl) lysine isopeptide bonds formed after 4 h of enzyme incubation was 2.21 μmol/g of protein. SDS-PAGE showed that the oat globulin acidic polypeptides (AP) were more susceptible to polymerization than the basic polypeptides (BP), and the reactivities of both AP and BP were enhanced by the addition of other substrate proteins. Differential scanning calorimetry showed that both the denaturation temperature and denaturation enthalpy were decreased after TG treatment. Fourier transform infrared spectroscopy revealed marked increases in the intensity of two intermolecular β-sheet bands associated with aggregate formation but little conformational changes in the polymerized protein. TG incubation led to progressive changes in flow properties of oat globulin dispersions, indicating enhanced pseudoplasticity and increased viscosity and yield stress.
Persistent Identifierhttp://hdl.handle.net/10722/68492
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSiu, NCen_HK
dc.contributor.authorMa, CYen_HK
dc.contributor.authorMine, Yen_HK
dc.date.accessioned2010-09-06T06:05:05Z-
dc.date.available2010-09-06T06:05:05Z-
dc.date.issued2002en_HK
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 2002, v. 50 n. 9, p. 2660-2665en_HK
dc.identifier.issn0021-8561en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68492-
dc.description.abstractOat globulin was polymerized by a microbial transglutaminase (TG), and some physicochemical and functional properties of polymers were studied. Reversed-phase HPLC revealed that the number of ε-(γ-glutamyl) lysine isopeptide bonds formed after 4 h of enzyme incubation was 2.21 μmol/g of protein. SDS-PAGE showed that the oat globulin acidic polypeptides (AP) were more susceptible to polymerization than the basic polypeptides (BP), and the reactivities of both AP and BP were enhanced by the addition of other substrate proteins. Differential scanning calorimetry showed that both the denaturation temperature and denaturation enthalpy were decreased after TG treatment. Fourier transform infrared spectroscopy revealed marked increases in the intensity of two intermolecular β-sheet bands associated with aggregate formation but little conformational changes in the polymerized protein. TG incubation led to progressive changes in flow properties of oat globulin dispersions, indicating enhanced pseudoplasticity and increased viscosity and yield stress.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.subjectDSCen_HK
dc.subjectFlow propertiesen_HK
dc.subjectFTIR spectroscopyen_HK
dc.subjectOat globulinen_HK
dc.subjectProtein polymerizationen_HK
dc.subjectStructural propertiesen_HK
dc.subjectTransglutaminaseen_HK
dc.titlePhysicochemical and structural properties of oat globulin polymers formed by a microbial transglutaminaseen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8561&volume=50&spage=2660&epage=2665&date=2002&atitle=Physicochemical+and+structural+properties+of+oat+globulin+polymers+formed+by+a+microbial+transglutaminaseen_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/jf0110304en_HK
dc.identifier.scopuseid_2-s2.0-0037165562en_HK
dc.identifier.hkuros68444en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037165562&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume50en_HK
dc.identifier.issue9en_HK
dc.identifier.spage2660en_HK
dc.identifier.epage2665en_HK
dc.identifier.isiWOS:000175168200032-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSiu, NC=7004303654en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.scopusauthoridMine, Y=7103350429en_HK

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