NDLI: Production of a recombinant chitin oligosaccharide deacetylase from Vibrio parahaemolyticus in the culture medium of Escherichia coli cells

Content Provider	Springer Nature Link
Author	Kadokura, Kazunari Sakamoto, Yusuke Saito, Kaori Ikegami, Takari Hira, Takako Hakamata, Wataru Oku, Tadatake Nishio, Toshiyuki
Copyright Year	2007
Abstract	An open reading frame (ORF) encoding chitin oligosaccharide deacetylase (Pa-COD) gene and its signal sequence was cloned from the Vibrio parahaemolyticus KN1699 genome and its sequence was analyzed. The ORF encoded a 427 amino acid protein, including the 22 amino acid signal sequence. The deduced amino acid sequence was highly similar to several bacterial chitin oligosaccharide deacetylases in carbohydrate esterase family 4. An expression plasmid containing the gene was constructed and inserted into Escherichia coli cells and the recombinant enzyme was secreted into the culture medium with the aid of the signal peptide. The concentration of the recombinant enzyme in the E. coli culture medium was 150 times larger than that of wild-type enzyme produced in the culture medium by V. parahaemolyticus KN1699. The recombinant enzyme was purified to homogeneity from culture supernatant in an overall yield of 16%. Substrate specificities of the wild-type and the recombinant enzymes were comparable.
Starting Page	1209
Ending Page	1215
Page Count	7
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	29
Issue Number	8
e-ISSN	15736776
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2007-05-04
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Chitin oligosaccharide deacetylase Escherichia coli Recombinant enzyme Signal peptide Vibrio parahaemolyticus Biochemistry Applied Microbiology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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