whereas
Aspergillus niger has high b-glucosidase activity but lower endoglucanase
levels, and hence it has limited efficiency in cellulosic hydrolysis.
The addition of b-glucosidase has shown to greatly increase
the performance of commercial cellulases in lignocellulose hydrolysis
(Barakat et al., 2012). Recent studies have also shown that
addition of purified endoglucanase to commercial cellulases caused
a stimulatory effect on hydrolysis of lignocellulosic biomass (Sujit
et al., 2013). The hydrolytic efficiency of a multi-cellulase complex
for lignocellulose saccharification depends on both the properties of
individual enzymes and their ratio in the enzyme cocktail. The inhouse
isolate Aspergillus terreus was able to produce a complete
enzyme system (EG, CBH, and BG) which hydrolyses highly ordered
cellulose and produce glucose as a major end product with high
saccharification efficiency (Narra et al., 2012).
The present study is focused on production, purification,
biochemical characterization and partial sequencing of a potential
endoglucanase from cellulose degrading fungus A. terreus. The
current investigation also demonstrates the synergetic effect of
purified endoglucanase with A. terreus crude cellulase for enzymatic
hydrolysis of mild alkali treated rice straw.