PRODUCTION, PURIFICATION AND CHARACTERIZATION OF GLUCOSE-OXIDASE FROMPENICILLIUM VARIABILE P16

Glucose oxidase was produced by Penicillium variabile P16 grown in a b enchtop bioreactor and purified 30-fold to homogeneity by ion-exchange and gel-filtration chromatography. The M(r) of the native enzyme was 126 000 and that of the subunit 62 000, which indicated that the nativ e enzyme is a dimer. The enzyme was optimally active at pH 6.0 and 55 degrees C and highly specific for beta-D-glucose (K-m 6.0 mM). Two iso enzymes, with pI values of 4.8-4.9, were detected on analytical isoele ctric-focusing gels. The glucose oxidase was severely inhibited by Cu2 + and Ag+ ions and, to a lower extent, by NaF.