Cloning, expression and purification of Bacillus cereus endochitinase in the Escherichia coli AD494(DE3)pLysS expression system.
نویسندگان
چکیده
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.
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عنوان ژورنال:
- Bioscience, biotechnology, and biochemistry
دوره 73 5 شماره
صفحات -
تاریخ انتشار 2009