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Article: Thermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: A comparative study

TitleThermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: A comparative study
Authors
KeywordsAmino Acid Composition
In Vitro Digestibility
Phaseolus Legume
Thermal Aggregation
Vicilin
Issue Date2009
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchem
Citation
Food Chemistry, 2009, v. 113 n. 4, p. 957-963 How to Cite?
AbstractThe heat-induced aggregation and the in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes, including kidney bean, red bean and mung bean were investigated and compared, and their amino acid composition and free sulfhydryl (SH) group contents also evaluated. The results showed that the extent in the heat-induced aggregation varied with the type of the protein isolates, and the formation of new disulphide bonds (at the expense of free SH contents) was involved in the formation of the aggregates. The protein isolates with higher levels of hydrophobic and uncharged polar amino acids, and lower basic amino acid contents exhibited lower extent of their heat-induced aggregation. The in vitro pepsin plus trypsin digestibility was different for various native protein isolates. The digestibility was to a varying extent affected by the heat treatment. The influences of heating on the digestibility of these proteins were closely related to the extent of their heat-induced aggregation. The results suggest that the improvement of nutritional property of those vicilin-rich protein isolates by heat treatment is largely dependent upon their amino acid composition as well as the extent of heat-induced aggregation. © 2008 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/179101
ISSN
2015 Impact Factor: 4.052
2015 SCImago Journal Rankings: 1.620
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTang, CHen_US
dc.contributor.authorChen, Len_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:51:59Z-
dc.date.available2012-12-19T09:51:59Z-
dc.date.issued2009en_US
dc.identifier.citationFood Chemistry, 2009, v. 113 n. 4, p. 957-963en_US
dc.identifier.issn0308-8146en_US
dc.identifier.urihttp://hdl.handle.net/10722/179101-
dc.description.abstractThe heat-induced aggregation and the in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes, including kidney bean, red bean and mung bean were investigated and compared, and their amino acid composition and free sulfhydryl (SH) group contents also evaluated. The results showed that the extent in the heat-induced aggregation varied with the type of the protein isolates, and the formation of new disulphide bonds (at the expense of free SH contents) was involved in the formation of the aggregates. The protein isolates with higher levels of hydrophobic and uncharged polar amino acids, and lower basic amino acid contents exhibited lower extent of their heat-induced aggregation. The in vitro pepsin plus trypsin digestibility was different for various native protein isolates. The digestibility was to a varying extent affected by the heat treatment. The influences of heating on the digestibility of these proteins were closely related to the extent of their heat-induced aggregation. The results suggest that the improvement of nutritional property of those vicilin-rich protein isolates by heat treatment is largely dependent upon their amino acid composition as well as the extent of heat-induced aggregation. © 2008 Elsevier Ltd. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchemen_US
dc.relation.ispartofFood Chemistryen_US
dc.subjectAmino Acid Compositionen_US
dc.subjectIn Vitro Digestibilityen_US
dc.subjectPhaseolus Legumeen_US
dc.subjectThermal Aggregationen_US
dc.subjectVicilinen_US
dc.titleThermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: A comparative studyen_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.foodchem.2008.08.038en_US
dc.identifier.scopuseid_2-s2.0-55949132286en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-55949132286&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume113en_US
dc.identifier.issue4en_US
dc.identifier.spage957en_US
dc.identifier.epage963en_US
dc.identifier.isiWOS:000261857100015-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridTang, CH=35197262700en_US
dc.identifier.scopusauthoridChen, L=7409435006en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

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