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Article: Transglutaminase-induced cross-linking of vicilin-rich kidney protein isolate: Influence on the functional properties and in vitro digestibility

TitleTransglutaminase-induced cross-linking of vicilin-rich kidney protein isolate: Influence on the functional properties and in vitro digestibility
Authors
KeywordsCross-Linking
Functional Property
In Vitro Digestibility
Kidney Protein Isolate
Transglutaminase
Issue Date2008
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodres
Citation
Food Research International, 2008, v. 41 n. 10, p. 941-947 How to Cite?
AbstractThe covalent cross-linking of vicilin-rich protein isolate from kidney bean (KPI) by microbial transglutraminase (MTGase; at an enzyme-substrate ratio of 5.0 units per gram protein) was characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and size exclusion chromatography combined with multi-angle laser light scattering (SEC-MALLS). Effects of MTGase treatment on some functional properties and in vitro trypsin digestibility of KPI were evaluated. SDS-PAGE and SEC-MALLS analyses indicated that MTGase polymerized the vicilin component in KPI to form high molecular weight oligomers or biopolymers, and the cross-linking occurred among intermolecular and intramolecular subunits. MTGase treatment led to a significant decrease in total free SH content and an increase in surface hydrophobicity, suggesting unfolding of the vicilin molecules. Protein solubility, emulsifying activity index, and emulsion stability index of KPI were progressively decreased with increasing MTGase incubation time. Thermal stability and in vitro trypsin digestibility of the vicilin component were gradually and significantly increased. These results suggest that functional properties of vicilin-rich KPI could be negatively affected by the enzymatic cross-linking, while nutritional property might be markedly enhanced. © 2008 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/179100
ISSN
2015 Impact Factor: 3.182
2015 SCImago Journal Rankings: 1.539
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTang, CHen_US
dc.contributor.authorSun, Xen_US
dc.contributor.authorYin, SWen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:51:58Z-
dc.date.available2012-12-19T09:51:58Z-
dc.date.issued2008en_US
dc.identifier.citationFood Research International, 2008, v. 41 n. 10, p. 941-947en_US
dc.identifier.issn0963-9969en_US
dc.identifier.urihttp://hdl.handle.net/10722/179100-
dc.description.abstractThe covalent cross-linking of vicilin-rich protein isolate from kidney bean (KPI) by microbial transglutraminase (MTGase; at an enzyme-substrate ratio of 5.0 units per gram protein) was characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and size exclusion chromatography combined with multi-angle laser light scattering (SEC-MALLS). Effects of MTGase treatment on some functional properties and in vitro trypsin digestibility of KPI were evaluated. SDS-PAGE and SEC-MALLS analyses indicated that MTGase polymerized the vicilin component in KPI to form high molecular weight oligomers or biopolymers, and the cross-linking occurred among intermolecular and intramolecular subunits. MTGase treatment led to a significant decrease in total free SH content and an increase in surface hydrophobicity, suggesting unfolding of the vicilin molecules. Protein solubility, emulsifying activity index, and emulsion stability index of KPI were progressively decreased with increasing MTGase incubation time. Thermal stability and in vitro trypsin digestibility of the vicilin component were gradually and significantly increased. These results suggest that functional properties of vicilin-rich KPI could be negatively affected by the enzymatic cross-linking, while nutritional property might be markedly enhanced. © 2008 Elsevier Ltd. All rights reserved.en_US
dc.languageengen_US
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodresen_US
dc.relation.ispartofFood Research Internationalen_US
dc.subjectCross-Linkingen_US
dc.subjectFunctional Propertyen_US
dc.subjectIn Vitro Digestibilityen_US
dc.subjectKidney Protein Isolateen_US
dc.subjectTransglutaminaseen_US
dc.titleTransglutaminase-induced cross-linking of vicilin-rich kidney protein isolate: Influence on the functional properties and in vitro digestibilityen_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.doi10.1016/j.foodres.2008.07.015en_US
dc.identifier.scopuseid_2-s2.0-55649086169en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-55649086169&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume41en_US
dc.identifier.issue10en_US
dc.identifier.spage941en_US
dc.identifier.epage947en_US
dc.identifier.isiWOS:000261485700001-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridTang, CH=35197262700en_US
dc.identifier.scopusauthoridSun, X=7405619919en_US
dc.identifier.scopusauthoridYin, SW=21234441700en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

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