Purification of beta-glucosidase from XXXX lactis strain Y-123.

@entity78 @entity7878 @entity692 @entity2975 @entity375 @entity1068 @entity1329
@entity375 lactis strain Y-123, a constitutive high producer of beta-glucosidase (B(h)), was grown in an enriched medium. beta-Glucosidase, extracted most easily by cell autolysis, was purified by successive @entity1329 precipitation, @entity1068 precipitation, gel filtration, @entity78 gel adsorption-elution, and @entity692 column chromatography. The specific activity of the enzyme increased 200-fold during the purification. The electrophoretic and catalytic properties of the enzyme did not change during the procedure. @entity2975 gel disc electrophoresis of the partially purified enzyme revealed one major and several minor protein-staining bands. beta-Glucosidase activity in the @entity2975 gel columns was measured directly by assaying sections of columns frozen and sliced immediately after electrophoresis. Most of the activity coincided with the major protein-staining band. Prolonged assay produced minor activity coinciding with the less intense protein bands. Properties of the enzyme suggest that it is a single, unconjugated, intracellular, high molecular weight protein. The purification procedure is applicable to strains of @entity7878 which possess alleles of the B locus for beta-glucosidase synthesis.
