File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Effect of deamidation and succinylation on some physicochemical and baking properties of gluten

TitleEffect of deamidation and succinylation on some physicochemical and baking properties of gluten
Authors
Issue Date1986
PublisherWiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-1147
Citation
Journal Of Food Science, 1986, v. 51 n. 1, p. 99-103 How to Cite?
AbstractVital wheat gluten was modified by deamidation and succinylation. Deamidation caused a progressive degradation of gliadin with concomitant increase in low molecular weight components, but glutenin was not affected. Deamidation also markedly increased the net negative charge and surface hydrophobicity of gluten, while the bread loaf volume and dough extensibility were decreased. The most significant change in physiochemical properties of gluten caused by succinylation was an increase in net negative charge. Succinylation led to a pronounced decrease in dough extensibility but no significant changes in specific loaf volume. The data indicated the importance of hydrogen bonding offered by the amide groups of gluten in the breadmaking process. Changes in molecular weight distribution and hydrophobic interaction may also affect the baking performance of gluten. Ionic interaction may be involved in dough development but is less critical in controlling the overall baking performance of gluten.
Persistent Identifierhttp://hdl.handle.net/10722/178382
ISSN
2015 Impact Factor: 1.649
2015 SCImago Journal Rankings: 0.839
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_US
dc.contributor.authorOomah, BDen_US
dc.contributor.authorHolme, Jen_US
dc.date.accessioned2012-12-19T09:47:22Z-
dc.date.available2012-12-19T09:47:22Z-
dc.date.issued1986en_US
dc.identifier.citationJournal Of Food Science, 1986, v. 51 n. 1, p. 99-103en_US
dc.identifier.issn0022-1147en_US
dc.identifier.urihttp://hdl.handle.net/10722/178382-
dc.description.abstractVital wheat gluten was modified by deamidation and succinylation. Deamidation caused a progressive degradation of gliadin with concomitant increase in low molecular weight components, but glutenin was not affected. Deamidation also markedly increased the net negative charge and surface hydrophobicity of gluten, while the bread loaf volume and dough extensibility were decreased. The most significant change in physiochemical properties of gluten caused by succinylation was an increase in net negative charge. Succinylation led to a pronounced decrease in dough extensibility but no significant changes in specific loaf volume. The data indicated the importance of hydrogen bonding offered by the amide groups of gluten in the breadmaking process. Changes in molecular weight distribution and hydrophobic interaction may also affect the baking performance of gluten. Ionic interaction may be involved in dough development but is less critical in controlling the overall baking performance of gluten.en_US
dc.languageengen_US
dc.publisherWiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-1147en_US
dc.relation.ispartofJournal of Food Scienceen_US
dc.titleEffect of deamidation and succinylation on some physicochemical and baking properties of glutenen_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.doi10.1111/j.1365-2621.1986.tb10845.xen_US
dc.identifier.scopuseid_2-s2.0-0001939449en_US
dc.identifier.volume51en_US
dc.identifier.issue1en_US
dc.identifier.spage99en_US
dc.identifier.epage103en_US
dc.identifier.isiWOS:A1986AYZ8800025-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridoomah, BD=7003307407en_US
dc.identifier.scopusauthoridHolme, J=55236317100en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats