Physical characterization of isozymes of endo-beta-1,4-glucanase and beta-1,4-glucosidase from Aspergillus species

FEMS Microbiol Lett. 1991 Mar 15;63(1):99-104. doi: 10.1016/0378-1097(91)90535-i.

Abstract

Electrophoretic data revealed the presence of various isozymes of endoglucanase and beta-glucosidase, the number of which varied from one to three in various species of the genus Aspergillus. pH 5.0 was optimum for all the isozymes whereas metal ion treatment showed complete inhibition of almost all the isozymes by Hg2+ and partial inhibition by Ca2+ and Co2+ of isozymes of both the enzymes. An alteration in the electrophoretic mobility of isozymes of beta-glucosidase was also noticed in some species with Hg2+ treatment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus / enzymology*
  • Calcium / pharmacology
  • Cellulase / antagonists & inhibitors
  • Cellulase / chemistry
  • Cellulase / metabolism*
  • Cobalt / pharmacology
  • Electrophoresis, Polyacrylamide Gel
  • Glucosidases / antagonists & inhibitors
  • Glucosidases / chemistry
  • Glucosidases / metabolism*
  • Hydrogen-Ion Concentration
  • Isoenzymes / antagonists & inhibitors
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism*
  • Mercury / pharmacology

Substances

  • Isoenzymes
  • Cobalt
  • Glucosidases
  • Cellulase
  • Mercury
  • Calcium