01723naa a2200229 a 450000100080000000500110000800800410001902400420006010000180010224500930012026000090021352010330022265300120125570000200126770000180128770000300130570000150133570000240135070000270137470000220140177300700142319280152022-04-04       2013    bl uuuu     u00u1 u    #d7 a10.1111/j.1745-4514.2011.00632.x2DOI1 aSANTOS, R. F.  aPurification and characterization of soy cotyledon B-glucosidase.h[electronic resource]  c2013  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.  aSoybean1 aOLIVEIRA, C. F.1 aVARÉA, G. S.1 aSILVA, M. L. C. ORRADI da1 aIDA, E. I.1 aMANDARINO, J. M. G.1 aCARRÃO-PANIZZI, M. C.1 aRIBEIRO, M. L. L.  tJournal of Food Biochemistrygv. 37, n. 3, p. 302-312, Jun. 2013.