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Article: Functional properties of oat globulin modified by a calcium-independent microbial transglutaminase

TitleFunctional properties of oat globulin modified by a calcium-independent microbial transglutaminase
Authors
KeywordsFunctional properties
Gelation, rheology
Oat globulin
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. 2666-2672 How to Cite?
AbstractOat globulin was modified by a calcium-independent microbial transglutaminase (TG). The TG-polymerized protein had higher solubility than the control at acidic pH and had improved water- and fat-binding properties. Incubation of 10% (w/v) oat globulin dispersions in the presence of TG at 37 °C led to the formation of a well-developed viscoelastic gel network with a microstructure characterized by thick strands and large clusters. The TG-induced gels had higher modulus values, lower loss tangent values, and lower frequency dependency than the heat-induced gels. The TG-induced gel system has the characteristics of classical polymer gel with permanent "chemical" cross-links, whereas the heat-denatured system has the characteristics of a temporary "physical" gel with breakable crosslinks. Fourier transform infrared spectroscopy showed marked shift and intensity changes in several major bands, suggesting pronounced changes in protein conformation during TG-induced gelation. Aggregation of protein molecules was also indicated by the progressive increases in two infrared bands (1679-1682 and 1622-1625 cm -1) associated with the formation of intermolecular β-sheets and strands. Results suggest that new food polymers with unique functionality can be produced from oat globulin treated with TG and that elastic gels can be formed near neutral pH, instead of the alkaline pH required for thermally induced oat globulin gels.
Persistent Identifierhttp://hdl.handle.net/10722/68703
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.authorMock, WYen_HK
dc.contributor.authorMines, Yen_HK
dc.date.accessioned2010-09-06T06:06:54Z-
dc.date.available2010-09-06T06:06:54Z-
dc.date.issued2002en_HK
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 2002, v. 50 n. 9, p. 2666-2672en_HK
dc.identifier.issn0021-8561en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68703-
dc.description.abstractOat globulin was modified by a calcium-independent microbial transglutaminase (TG). The TG-polymerized protein had higher solubility than the control at acidic pH and had improved water- and fat-binding properties. Incubation of 10% (w/v) oat globulin dispersions in the presence of TG at 37 °C led to the formation of a well-developed viscoelastic gel network with a microstructure characterized by thick strands and large clusters. The TG-induced gels had higher modulus values, lower loss tangent values, and lower frequency dependency than the heat-induced gels. The TG-induced gel system has the characteristics of classical polymer gel with permanent "chemical" cross-links, whereas the heat-denatured system has the characteristics of a temporary "physical" gel with breakable crosslinks. Fourier transform infrared spectroscopy showed marked shift and intensity changes in several major bands, suggesting pronounced changes in protein conformation during TG-induced gelation. Aggregation of protein molecules was also indicated by the progressive increases in two infrared bands (1679-1682 and 1622-1625 cm -1) associated with the formation of intermolecular β-sheets and strands. Results suggest that new food polymers with unique functionality can be produced from oat globulin treated with TG and that elastic gels can be formed near neutral pH, instead of the alkaline pH required for thermally induced oat globulin gels.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.subjectFunctional propertiesen_HK
dc.subjectGelation, rheologyen_HK
dc.subjectOat globulinen_HK
dc.subjectTransglutaminaseen_HK
dc.titleFunctional properties of oat globulin modified by a calcium-independent microbial transglutaminaseen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8561&volume=50&spage=2666&epage=2672&date=2002&atitle=Functional+properties+of+oat+globulin+modified+by+a+calcium-independent+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/jf011163pen_HK
dc.identifier.pmid11958639-
dc.identifier.scopuseid_2-s2.0-0037165563en_HK
dc.identifier.hkuros68445en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037165563&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume50en_HK
dc.identifier.issue9en_HK
dc.identifier.spage2666en_HK
dc.identifier.epage2672en_HK
dc.identifier.isiWOS:000175168200033-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSiu, NC=7004303654en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.scopusauthoridMock, WY=7005314640en_HK
dc.identifier.scopusauthoridMines, Y=39461856800en_HK

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