Properties of exoglucanase from aspergillus niger

Abstract

Exoglucanase (EC 3.2.1.91) was partially purified from Aspergillus niger. The enzyme was stable at room temperature in the pH range of 4.0-6.0 for 24 h, with the optimum at 5.5. The enzyme had an optimum temperature of 50°C and a tl/2at 65°C was 70 min. Kmand Vmaxvalues were found to be 55.5 mg/ml and 0.9/μM/min, respectively. Glycerol protected the enzyme from inactivation on storage and from denaturation due to freezing and thawing. The effect of the sulfhydryl group reagents tested suggested the presence of -SH on the active site of the enzyme. Mn2+ and Co2+ were good activators of the enzyme, whereas Hg2+ and Pb2+ were potent inhibitors. The enzyme was a metalloprotein, or it requires certain metal ions for activation. © 1990, Applied Microbiology, Molecular and Cellular Biosciences Research Foundation. All rights reserved.