[Purification and properties of beta-glucosidase from Aspergillus phoenicis].
A beta-glucosidase has been purified to electrophoretically homogeneity from the wheat bran culture of Aspergillus phoenicis by PEG 6000-phosphate biphasic separation, column chromatography on Sephadex G-100, DEAE-Sephadex A-50 and SE-Sephadex C-50. The enzyme showed optimal activity at pH 5.0 and 60 degrees C. It was stable in the pH range of 4.0-7.5 and up to 55 degrees C. The enzyme activity was strongly inhibited by Ag+ and Hg2+. The molecular weight of the enzyme was 118000 as determined by SDS-PAGE and 195000 by gradient-PAGE. The isoelectric point was pI 3.95 as determined by PAGIF.
Zeng
Y C
YC
Zhang
S Z
SZ
D001230:Aspergillus / Q000201:enzymology*; D005959:Glucosidases / Q000302:isolation & purification*; D001617:beta-Glucosidase / Q000302:isolation & purification*
D005959:Glucosidases; D001617:beta-Glucosidase