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 | Acesso ao texto completo restrito à biblioteca da Embrapa Soja. Para informações adicionais entre em contato com valeria.cardoso@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Soja. |
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Data corrente: |
10/07/2012 |
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Data da última atualização: |
04/04/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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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. |
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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. |
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Título: |
Purification and characterization of soy cotyledon B-glucosidase. |
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Ano de publicação: |
2013 |
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Fonte/Imprenta: |
Journal of Food Biochemistry, v. 37, n. 3, p. 302-312, Jun. 2013. |
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DOI: |
10.1111/j.1745-4514.2011.00632.x |
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Idioma: |
Inglês |
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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. |
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Palavras-Chave: |
Soybean. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 01723naa a2200229 a 4500
001 1928015
005 2022-04-04
008 2013 bl uuuu u00u1 u #d
024 7 $a10.1111/j.1745-4514.2011.00632.x$2DOI
100 1 $aSANTOS, R. F.
245 $aPurification and characterization of soy cotyledon B-glucosidase.$h[electronic resource]
260 $c2013
520 $ab-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.
653 $aSoybean
700 1 $aOLIVEIRA, C. F.
700 1 $aVARÉA, G. S.
700 1 $aSILVA, M. L. C. ORRADI da
700 1 $aIDA, E. I.
700 1 $aMANDARINO, J. M. G.
700 1 $aCARRÃO-PANIZZI, M. C.
700 1 $aRIBEIRO, M. L. L.
773 $tJournal of Food Biochemistry$gv. 37, n. 3, p. 302-312, Jun. 2013.
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