Please use this identifier to cite or link to this item: http://cmuir.cmu.ac.th/jspui/handle/6653943832/60158
Title: Cloning and expression of chitinase A gene from Streptomyces cyaneus SP-27: The enzyme participates in protoplast formation of Schizophyllum commune
Authors: Shigekazu Yano
Arata Honda
Nopakarn Rattanakit
Yuta Noda
Mamoru Wakayama
Abhinya Plikomol
Takashi Tachiki
Keywords: Biochemistry, Genetics and Molecular Biology
Chemistry
Immunology and Microbiology
Issue Date: 30-Jul-2008
Abstract: Chitinase A of Streptomyces cyaneus SP-27 or chitinase I of Bacillus circulans KA-304 showed the protoplast-forming activity when combined with α-1,3-glucanase of B. circulans KA-304. The gene of chitinase A was cloned. It consisted of 903 nucleotides encoding 301 amino acid residues, including a putative signal peptide (35 amino acid residues). The deduced N-terminal moiety of chitinase A showed sequence homology with the chitin-binding domain of chitinase F from Streptomyces coelicolor and chitinase 30 from Streptomyces olivaceoviridisis. The C-terminal moiety also showed high sequence similarity to the catalytic domain of several Streptomyces family 19 chitinases as well as that of chitinase I of B. circulans KA-304. Recombinant chitinase A was expressed in Escherichia coli Rosetta-gami B (DE 3). The properties of the recombinant enzyme were almost the same as those of chitinase A purified from a culture filtrate of S. cyaneus SP-27. The recombinant enzyme was superior to B. circulans KA-304 chitinase I not only in respect to protoplast forming activity in a mixture containing α-1,3-glucanase, but also to antifungal activity and powder chitin-hydrolyzing activity.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=47949114147&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/60158
ISSN: 13476947
09168451
Appears in Collections:CMUL: Journal Articles

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