Produção Nacional
Revisado por pares
PURIFICATION AND CHARACTERIZATION OF SOY COTYLEDON β-GLUCOSIDASE
2012; Wiley; Volume: 37; Issue: 3 Linguagem: Inglês
10.1111/j.1745-4514.2011.00632.x
ISSN1745-4514
AutoresRamón Santos, Camila Fogaça de Oliveira, Geni Silva Varéa, M.L.C. ORRADI DA SILVA, Elza Iouko Ida, J. M. G. Mandarino, M.C. CARRÃO-PANIZZI, Mara Lúcia Luiz Ribeiro,
Tópico(s)Natural Antidiabetic Agents Studies
ResumoJournal of Food BiochemistryVolume 37, Issue 3 p. 302-312 Full Article PURIFICATION AND CHARACTERIZATION OF SOY COTYLEDON β-GLUCOSIDASE R.F. SANTOS, R.F. SANTOS Biochemistry and Biotechnology Department, Universidade Estadual de Londrina. Caixa Postal 6001, CEP 86.051-990, Londrina, PR, BrazilSearch for more papers by this authorC.F. OLIVEIRA, C.F. OLIVEIRA Biochemistry and Biotechnology Department, Universidade Estadual de Londrina. Caixa Postal 6001, CEP 86.051-990, Londrina, PR, BrazilSearch for more papers by this authorG.S. VARÉA, G.S. VARÉA Biochemistry and Biotechnology Department, Universidade Estadual de Londrina. Caixa Postal 6001, CEP 86.051-990, Londrina, PR, BrazilSearch for more papers by this authorM.L.C. ORRADI DA SILVA, M.L.C. ORRADI DA SILVA Carbohydrate Biochemistry Laboratory, Physics, Chemistry and Biology Department, Science and Technology College, UNESP – Presidente Prudente, SP, BrazilSearch for more papers by this authorE.I. IDA, E.I. IDA Food Technology and Science Department, Universidade Estadual de Londrina. Caixa Postal 6001, Londrina, PR, BrazilSearch for more papers by this authorJ.M.G. MANDARINO, J.M.G. MANDARINO Embrapa (Brazilian Enterprise for Agricultural Research)–Nacional Soy Research Center (CNPSo), Londrina, PR, BrazilSearch for more papers by this authorM.C. CARRÃO-PANIZZI, M.C. CARRÃO-PANIZZI Embrapa (Brazilian Enterprise for Agricultural Research)–Nacional Soy Research Center (CNPSo), Londrina, PR, BrazilSearch for more papers by this authorM.L.L. RIBEIRO, Corresponding Author M.L.L. RIBEIRO Biochemistry and Biotechnology Department, Universidade Estadual de Londrina. Caixa Postal 6001, CEP 86.051-990, Londrina, PR, Brazil TEL: 55-43-3371-4270; FAX: 55-43-3371-4270; EMAIL: [email protected]Search for more papers by this author R.F. SANTOS, R.F. SANTOS Biochemistry and Biotechnology Department, Universidade Estadual de Londrina. Caixa Postal 6001, CEP 86.051-990, Londrina, PR, BrazilSearch for more papers by this authorC.F. OLIVEIRA, C.F. OLIVEIRA Biochemistry and Biotechnology Department, Universidade Estadual de Londrina. Caixa Postal 6001, CEP 86.051-990, Londrina, PR, BrazilSearch for more papers by this authorG.S. VARÉA, G.S. VARÉA Biochemistry and Biotechnology Department, Universidade Estadual de Londrina. Caixa Postal 6001, CEP 86.051-990, Londrina, PR, BrazilSearch for more papers by this authorM.L.C. ORRADI DA SILVA, M.L.C. ORRADI DA SILVA Carbohydrate Biochemistry Laboratory, Physics, Chemistry and Biology Department, Science and Technology College, UNESP – Presidente Prudente, SP, BrazilSearch for more papers by this authorE.I. IDA, E.I. IDA Food Technology and Science Department, Universidade Estadual de Londrina. Caixa Postal 6001, Londrina, PR, BrazilSearch for more papers by this authorJ.M.G. MANDARINO, J.M.G. MANDARINO Embrapa (Brazilian Enterprise for Agricultural Research)–Nacional Soy Research Center (CNPSo), Londrina, PR, BrazilSearch for more papers by this authorM.C. CARRÃO-PANIZZI, M.C. CARRÃO-PANIZZI Embrapa (Brazilian Enterprise for Agricultural Research)–Nacional Soy Research Center (CNPSo), Londrina, PR, BrazilSearch for more papers by this authorM.L.L. RIBEIRO, Corresponding Author M.L.L. RIBEIRO Biochemistry and Biotechnology Department, Universidade Estadual de Londrina. Caixa Postal 6001, CEP 86.051-990, Londrina, PR, Brazil TEL: 55-43-3371-4270; FAX: 55-43-3371-4270; EMAIL: [email protected]Search for more papers by this author First published: 08 June 2012 https://doi.org/10.1111/j.1745-4514.2011.00632.xCitations: 5Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Abstract ABSTRACT β-Glucosidase F42 of soy cotyledons was purified by ammonium sulfate fractionation, ion-exchange chromatography (CM-Sephadex-C-50, Sigma, St. Louis, MO) and gel filtration (Sephadex G-100, Sigma). The enzyme was purified 111.8-fold relative to its concentration in the crude extract. It had an apparent molecular mass of 53 kDa in gel filtration experiments and produced a 33-kDa band in sodium dodecyl sulfate–polyacrylamide gel electrophoresis, suggesting that it is dimeric. The purified β-glucosidase F42 was characterized as a glycoprotein after the identification of fucose, galactosamine and glucosamine by high-pressure anion-exchange chromatography–pulsed amperometric detector. Its highest activity was observed at pH 5.0 and 45C, and it was stable for up to 4 days at 25C. The Km of the enzyme was 0.12 mM p-nitrophenyl-β-d-glucopyranoside. β-Glucosidase F42 showed specificity for different substrates, and its activity was inhibited by 1 mM HgCl2, 10 mM glucono-δ-lactone or 150 mM glucose and increased by 10 mM MnCl2. PRACTICAL APPLICATIONS β-Glucosidase is an enzyme that hydrolyzes β-glucosidic bonds to liberate glucose and hydrolyzes isoflavones to release aglycones. Soy aglycones have been broadly investigated because of their biological activity in the prevention and treatment of some chronic diseases. Soy β-glucosidase can be used in the food industry to alter soy isoflavones for the production of functional foods that are rich in aglycone isoflavones. Therefore, it was an established method of purification of the enzyme that has great biotechnological potential. Citing Literature Volume37, Issue3June 2013Pages 302-312 RelatedInformation
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