Kinetics, Improved Activity and Thermostability of Endoglucanase and β-Glucosidase from a mutant-Derivative of Aspergillus niger MS82 (original) (raw)

Abstract

A mutant MS301 of Aspergillus niger MS82 showed 1.5 to 2.5-fold improved endoglucanase and β-glucosidase activity when grown on crude lignocellulosic substrates under solid-state and submerged conditions. Indicators of thermal stability of enzymes (T m and T 1/2) showed that the wild type and mutant endoglucanase was more heat-resistant compared to β-glucosidase. However, mutant and parent enzymes shared almost the same values for melting temperatures and half-lives. Endoglucanase and β-glucosidase from both the strains showed optimum activity under acidic pH. Energy of activation (Ea) of mutant β-glucosidase was substantially lower than the parent enzyme while E a of mutant endoglucanase was slightly less than the parent. The lowered E a values can be attributed to the improved β-glucosidase activity of the mutant strain. Moreover, the MS301 enzymes were better in hydrolyzing purified and crude cellulosic materials than the parent MS82. Introduction Lignocellulosic biomass constitu...

Ahmed Shakeel hasn't uploaded this paper.

Let Ahmed know you want this paper to be uploaded.

Ask for this paper to be uploaded.