ISOLATION AND SEPARATION OF β-GALACTOSIDASE FROM ASPERGILLUS NIDULANS

Abstract

Resolution  of  beta-galactosidase  of  Aspergilluc  nidulans  on  DEAE-cellulose revealed two peaks of  enzyme activity—designated as Enz A (the 0.2 M NaC1 eluted fraction) and Enz B (the 01 M NaC1  eluted fraction).  Ent A was obtained in larger yields and possessed higher activity than  Fr17  B.  Purification achieved with Enz A was 10-73 fold while that of Enz B was 1-56 fold only.  Some of  the kinetic studies undertaken with Enz A have been reported here.  Our evidences do not indicate  that the two enzyme fractions are different molecular forms of beta-galactosidase.