Cloning, expression and purification of Bacillus cereus endochitinase in the Escherichia coli AD494(DE3)pLysS expression system.
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-beta-(GlcNAc)(3) than to pNP-beta-(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.
Department of Food Science, National Taiwan Ocean University, Keelung, Taiwan.
Wei-Ming
WM
Chen
Gen-Hung
GH
Chen
Ching-San
CS
Chen
Shann-Tzong
ST
Jiang
D000595:Amino Acid Sequence; D001409:Bacillus cereus / Q000201:enzymology*; D001483:Base Sequence; D002688:Chitinases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification* / Q000378:metabolism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D008969:Molecular Sequence Data
D002688:Chitinases