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dc.contributor.authorElaine Sormus de Castro Pinto, Silvia [UNESP]
dc.contributor.authorNeves, Valdir Augusto [UNESP]
dc.contributor.authorMachado de Medeiros, Beatriz Maria [UNESP]
dc.date.accessioned2014-05-20T13:23:39Z
dc.date.available2014-05-20T13:23:39Z
dc.date.issued2009-02-11
dc.identifierhttp://dx.doi.org/10.1021/jf803108c
dc.identifier.citationJournal of Agricultural and Food Chemistry. Washington: Amer Chemical Soc, v. 57, n. 3, p. 1070-1075, 2009.
dc.identifier.issn0021-8561
dc.identifier.urihttp://hdl.handle.net/11449/7165
dc.description.abstractWe investigated the effects of treatments with the enzymes pepsin and trypsin on the in vitro immunological reactivity of the major globulins found in the seeds of sweet lupin, chickpea, and lentil. Polyclonal major globulin-specific antiserum was obtained by immunization of rabbits with a solution of the 11 S globulin of each legume. The globulins were hydrolyzed with pepsin and trypsin for 1, 5, 15, and 30 min. The native globulins and their hydrolysates were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting to identify the polypeptide bands with antigenic activity, and the hypoantigenicity of the hydrolysates was analyzed by enzyme-linked immunosorbent assay. Our results show that enzymatic treatment of the major storage protein (11 S globulin) of sweet lupin, chickpea, and lentil with pepsin or trypsin lead to the formation of large amounts of short peptides and free amino acids that do not allow antibody binding, resulting in a weakened immunoreactivity.en
dc.format.extent1070-1075
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal of Agricultural and Food Chemistry
dc.sourceWeb of Science
dc.subjectSweet lupinen
dc.subjectchickpeaen
dc.subjectlentilen
dc.subjectenzymatic hydrolysisen
dc.subjectantigenic activityen
dc.titleEnzymatic Hydrolysis of Sweet Lupin, Chickpea, and Lentil 11S Globulins Decreases their Antigenic Activityen
dc.typeArtigo
dcterms.licensehttp://pubs.acs.org/page/policy/nih/index.html
dcterms.rightsHolderAmer Chemical Soc
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.description.affiliationUNESP, Sch Pharmaceut Sci, Dept Biol Sci, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUNESP, Sch Pharmaceut Sci, Dept Food & Nutr, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUnespUNESP, Sch Pharmaceut Sci, Dept Biol Sci, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUnespUNESP, Sch Pharmaceut Sci, Dept Food & Nutr, BR-14801902 Araraquara, SP, Brazil
dc.identifier.doi10.1021/jf803108c
dc.identifier.wosWOS:000263042800042
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
dc.identifier.lattes4031319519910419
unesp.author.lattes4031319519910419
dc.relation.ispartofjcr3.412
dc.relation.ispartofsjr1,269
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