Expression, purification and characterization of a recombinant beta-glucosidase from Volvariella Volvacea.
For the first time, a beta-glucosidase gene from the edible straw mushroom, Volvariella volvacea V1-1, has been over-expressed in E. coli. The gene product was purified by chromatography showing a single band on SDS-PAGE. The recombinant enzyme had a molecular mass of 380 kDa with subunits of 97 kDa. The maximum activity was at pH 6.4 and 50 degrees C over a 5 min assay. The purified enzyme was stable from pH 5.6-8.0, had a half life of 1 h at 45 degrees C. The beta-glucosidase had a K(m) of 0.2 mM: for p-nitrophenyl-beta-D: -glucopyranoside.
Li
Xun
X
The Key Laboratory of Microbial Engineering, Nanjing Normal University, 210097, Nanjing, China.
Pei
Jianjun
J
Wu
Guogan
G
Shao
Weilan
W
D000363:Agaricales / Q000201:enzymology* / Q000235:genetics; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature; D001617:beta-Glucosidase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D011994:Recombinant Proteins; D001617:beta-Glucosidase