Thermostable B-1,4-glucosidase from thermotoga petrophila displaying highest ever reported enzyme Activity

Abstract

A thermostable novel ß- 1,4-glucosidase from Thermotoga petrophila (BglA) nucleotide sequence encoding the mature, monomeric protein cloned in a mesophilic host Escherichia coli BL21 CodonPlus (DE3)-RIPL and methods for over expression of this ß - glucosidase is provided. The purified extracellular enzyme was optimally active at pH 7.0 and 90°C with highly specific activity of 60714 U / mg against pNPG substrate. Purified enzyme displayed great substrate specific activity against p-nitrophenyl substrates and cellobiose. Because of its high thermostability, activity and apparent resistance against heavy metal ions, this enzyme may be a potential candidate for applications to convert lignocellulosic biomass to biofuels and various industrial applications.