A novel beta-1,4 glucanase produced by symbiotic Bacillus sp. CF96 isolated from termite (Anacanthotermes).

A novel beta-1,4-glucanase was purified and characterized from symbiotic Bacillus sp. CF96 of termite. The SDS-PAGE and zymogram analyses revealed a molecular mass of 35.6 kDa. Optimal activity was at 50 °C and pH 5.5, while the enzyme was active over a wide range of temperature 20-80 °C and pH 4-10 and interestingly more than 60% of the maximum activity remained up to pH 9. The enzyme activity increased in the presence of hexane, chloroform and methanol (20% v/v). while, the enzyme activity was inhibited by metal ions such as Mn2+, Hg2+, Cu2+, Zn2+, Mg2+, Fe2+. The isolated enzyme was able to degrade carboxymethyl cellulose (CMC), avicel and cellulose. Cellobiose was the hydrolytic product of enzymatic reaction based on thin layer chromatography (TLC) analysis. Regarding beta-1,4 endo/exoglucanase activity and high temperature, pH and solvent stability, the enzyme has potential for various industrial applications especially in designing pesticide for termite.