Cloning, Expression and Purification of Bacillus cereus Endochitinase in the Escherichia coli AD494(DE3)pLysS Expression System

Abstract

A chitinase gene from Bacillus cereus was cloned and expressed in Escherichia coli. The purified recombinant chitinase had much higher (128 fold) specificity to pNP-β-(GlcNAc)₃ than to pNP-β-(GlcNAc), suggesting endochitinase. Thirty-three amino acids in the N-terminal were recognized and cut off during expression, which consequently made the M_r not correspond to that predicted.