Data/hora: 09/06/2024 20:12:55

Biblioteca(s): | Embrapa Soja.
Data corrente: | 10/07/2012
Data da última atualização: | 04/04/2022
Autoria: | SANTOS, R. F.; OLIVEIRA, C. F.; VARÉA, G. S.; SILVA, M. L. C. ORRADI da; IDA, E. I.; MANDARINO, J. M. G.; CARRÃO-PANIZZI, M. C.; RIBEIRO, M. L. L.
Afiliação: | R. F. SANTOS, UEL; C. F. OLIVEIRA, UEL; G. S. VARÉA, UEL; M. L. C. ORRADI DA SILVA, UNESP Presidente Prudente; ELZA I. IDA, UEL; JOSE MARCOS GONTIJO MANDARINO, CNPSO; MERCEDES CONCORDIA CARRAO PANIZZI, CNPSo; M. L. L. RIBEIRO, UEL.
Título: | Purification and characterization of soy cotyledon B-glucosidase.
Ano de publicação: | 2013
Fonte/Imprenta: | Journal of Food Biochemistry, v. 37, n. 3, p. 302-312, Jun. 2013.
DOI: | 10.1111/j.1745-4514.2011.00632.x
Idioma: | Inglês
Conteúdo: | b-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 b-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 mMp-nitrophenyl-b-d-glucopyranoside. b-Glucosidase F42 showed specificity for different substrates, and its activity was inhibited by 1 mM HgCl2, 10mM glucono-d-lactone or 150 mMglucose and increased by 10 mMMnCl2.
Palavras-Chave: | Soybean.
Categoria do assunto: | --
Registro original: | Embrapa Soja (CNPSO)
Exemplares: | CNPSO - (33211-1) - UPC - AP - DD -  -  -  - DIS