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-β-(GlcNAc) 3 than to pNP-β-(GlcNAc), suggesting endochitinase. Thirty-three amino acids in the N-terminal were recognized and cut off d...

Full description

Saved in:
Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2009-05, Vol.73 (5), p.1172-1174
Main Authors: Chen, W.M.(National Taiwan Ocean Univ., Keelung), Chen, G.H, Chen, C.S, Jiang, S.T
Format: Article
Language:English
Subjects:
Amino Acid Sequence
BACILLUS CEREUS
Bacillus cereus - enzymology
Base Sequence
Biological and medical sciences
CHITINASE
Chitinases - biosynthesis
Chitinases - chemistry
Chitinases - genetics
Chitinases - isolation & purification
Chitinases - metabolism
CLONACION MOLECULAR
CLONAGE MOLECULAIRE
Cloning, Molecular
endochitinase
Escherichia coli
Escherichia coli - genetics
EXPRESION GENICA
EXPRESSION DES GENES
Fundamental and applied biological sciences. Psychology
GENE
GENE EXPRESSION
GENES
MOLECULAR CLONING
Molecular Sequence Data
PURIFICACION
PURIFICATION
QUITINASA
recognition peptide
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.80618