Cloning, Expression and Purification ofBacillus cereusEndochitinase in theEscherichia coliAD494(DE3)pLysS Expression System | Zendy

WeiMing Chen | Zendy; GenHung Chen | Zendy; Ching-San Chen | Zendy; ShannTzong Jiang | Zendy

Open Access

Cloning, Expression and Purification ofBacillus cereusEndochitinase in theEscherichia coliAD494(DE3)pLysS Expression System

Author(s) -

WeiMing Chen,

GenHung Chen,

Ching-San Chen,

ShannTzong Jiang

Publication year - 2009

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.80618

Subject(s) - bacillus cereus , escherichia coli , chitinase , recombinant dna , cloning (programming) , biology , microbiology and biotechnology , molecular cloning , gene , gene expression , biochemistry , bacteria , genetics , computer science , programming language

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research