Open AccessPurification and properties of a β‐glucosidase from Penicillium oxalicum autolysates
Author(s) -
CopaPatiño JoséLuis,
Rodriguez Juana,
Isabel PérezLeblic María
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb13861.x
Subject(s) - hydrolysis , concanavalin a , enzyme , chromatography , chemistry , homogeneous , penicillium , tannic acid , adsorption , biochemistry , food science , organic chemistry , in vitro , physics , thermodynamics
A β‐glucosidase from the medium of an autolyzed culture of Penicillium oxalicum has been purified by tannic acid precipitation, sephacryl S‐200, DEAE‐Biogel, CM‐Biogel and Mono Q successively. The purification process produced a homogeneous band in the SDS‐PAGE that correspond to a M r of 133 500. The enzyme had a pl of 4, and the active optima were found at pH 5.5 and 55°C. The enzyme hydrolyzed different different substrates showing maximum affinity againts p ‐nitrophenyl‐β‐ d ‐glucoside with a K m value of 0.37 mM. The β‐glucosidase was inhibited by Glucono‐ d ‐lactone but not by glucose in the concentration range of 1 to 10 mM. The enzyme was adsorbed by Concanavalin‐A‐Sepharose.