The Vicilin protein (Vigna radiata L.) of mung bean as a functional food Evidence of in vitro hypocholesterolemic activity

dc.contributor.authorAmaral, Ana Lucia [UNESP]
dc.contributor.authorFerreira, Ederlan Souza
dc.contributor.authorSilva, Maraiza Aparecida [UNESP]
dc.contributor.authorNeves, Valdir Augusto [UNESP]
dc.contributor.authorDemonte, Aureluce [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal da Bahia (UFBA)
dc.date.accessioned2018-11-26T17:42:26Z
dc.date.available2018-11-26T17:42:26Z
dc.date.issued2017-01-01
dc.description.abstractPurpose - The hypocholesterolemic activity of legume vicilins and the structural homology among mung bean, soybean and adzuki bean vicilins (8S) suggest that this protein may play a role in lipid metabolism. Thus, in the present study, the authors aim to isolate the mung bean vicilin and assess its in vitro effect on 3-hydroxy-3-methyl-glutaryl-CoA reductase (HMGCoAr), the enzyme responsible for endogenous cholesterol synthesis. Design/methodology/approach - Chromatographic and electrophoretic characterization identified the molecular mass and polypeptide composition of mung bean vicilin. The hydrolysate of this globulin was obtained by sequential hydrolysis with pepsin-pancreatin and the fragments were characterized by molecular filtration, SDS PAGE and HPLC. Findings - The molecular mass of vicilin was estimated as 158.23 at 6 10 kDa and SDS-PAGE revealed that the 8S globulin protein comprises four bands corresponding to polypeptides of 61, 48, 29 and 26 kDa. Fractions 10, 12, 14, 22 and 32 of the eluate from Sephadex G-25 exhibited significant inhibition of HMG CoAr. Originality/value - The correspondence of the chromatographic profile of the peptide fractions with hypocholesterolemic activity suggests that the composition and chemical structure of these peptides are essential to their physiological effectiveness. The beneficial effects of mung bean vicilin identified in this study will support the characterization of this protein as a functional compound.en
dc.description.affiliationSao Paulo State Univ, Dept Food & Nutr, Sch Pharmaceut Sci, Araraquara, Brazil
dc.description.affiliationUniv Fed Bahia, Dept Bromatol Anal, Sch Pharm, Salvador, BA, Brazil
dc.description.affiliationSao Paulo State Univ, Araraquara, Brazil
dc.description.affiliationUnespSao Paulo State Univ, Dept Food & Nutr, Sch Pharmaceut Sci, Araraquara, Brazil
dc.description.affiliationUnespSao Paulo State Univ, Araraquara, Brazil
dc.format.extent907-916
dc.identifierhttp://dx.doi.org/10.1108/NFS-05-2017-0089
dc.identifier.citationNutrition & Food Science. Bingley: Emerald Group Publishing Ltd, v. 47, n. 6, p. 907-916, 2017.
dc.identifier.doi10.1108/NFS-05-2017-0089
dc.identifier.fileWOS000416585000012.pdf
dc.identifier.issn0034-6659
dc.identifier.urihttp://hdl.handle.net/11449/163539
dc.identifier.wosWOS:000416585000012
dc.language.isoeng
dc.publisherEmerald Group Publishing Ltd
dc.relation.ispartofNutrition & Food Science
dc.relation.ispartofsjr0,248
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subject8S globulin
dc.subjectFunctional compound
dc.subjectHMG CoAr
dc.subjectHypocholesterolemic activity
dc.subjectMung bean
dc.titleThe Vicilin protein (Vigna radiata L.) of mung bean as a functional food Evidence of in vitro hypocholesterolemic activityen
dc.typeArtigo
dcterms.rightsHolderEmerald Group Publishing Ltd

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