An endo-beta-D-glycosidase from salivary glands of Macrotermes subhyalinus little soldier with a dual activity against carboxymethylcellulose and xylan

This study highlights an endo-beta-D-glycosidase from little soldier of Macrotermes subhyalinus purified by anion exchange, cation exchange and hydrophobic interaction chromatography. The only substrates that were hydrolyzed by the purified enzyme were xylans and carboxyméthylcellulose. The enzyme showed a single protein band and its relative molecular weight was estimated to be 215.45±5.63 kDa. The specific activities towards carboxymethylcellulose and xylan from Birchwood were respectively 9.32±3.78 and 8.59±2.54 U/ mg of protein. The purified enzyme showed an optimum pH of 4.6 for cellulase activity an 5.0 for xylanase activity in acetate buffer. The optimum temperature of the enzyme with CMC and xylan from Birchwood hydrolysis were found to be 60 and 55 °C respectively.