Isolation and Characterization of a Novel Acidophilic, Halotolerant and Cold-adaptive Cellulase (CMCase) from a Native Isolate Bacillus sp.

Abstract

A cold-adaptive acidic cellulase enzyme was produced by native Bacillus sp. TG-1 from Adana-TURKEY and the cellulase producing bacteria and the enzyme was characterized. In SDS-PAGE analysis the enzyme showed single bond of 52.4 kDa. The cellulase TG-1 had a pH optimum of 4.6 and displayed maximum activity at 45ºC. The enzyme was stable at pH ranging from 4.0 to 9.0 with more than 85% of original activity for 24 h. Also, the enzyme showed 100% stability at 20-40ºC for 60 min and exhibited more than 63% of maximum activity in different NaCl concentrations. The enzyme showed up to 70% stability against detergents and chelators, while it was strongly inhibited by Urea, H2O2, PMSF and 1,10-Phenanthroline and induced by β-mercaptoethanol and MnCl2. TLC analyses of the hydrolysis of Carboxymethyl cellulose (CMC) by the enzyme, revealed the presence of maltose and etc.