Molecular cloning and sequence analysis of the endochitinase from Chaetomium cupreum

Author

Zhang, Haiyan ; Ji, Hongfang ; Zhang, Lingwen ; Wu, Xingquan ; Chen, Shihua

Volume

4

fYear

2010

fDate

16-18 Oct. 2010

Firstpage

1707

Lastpage

1709

Abstract

Endochitinase gene fragment of Chaetomium cupreum (designated Chi46) obtained by construction of C. cupreum mycelium cDNA library. Its full-length cDNA was cloned by PCR. The results showed that the open reading frame of Chi46 was 1350bp and encoded a putative protein of 449 amino acids residues with s molecular mass of 46kDa. Bioinformatics analysis revealed that protein sequence of Chi46 containing a 22-residue secretion signal sequence and had a high degree of similarity with C. globosum chitinase. The domain search program at the NCBI and Pfam server showed that Chi46 protein had the glycosyl-hydrolase-18 conserved domain. Additionally, the deduced amino acid sequence had the same catalytic domain and substrate binding site with ech42 of Trichoderma harzianum.

Keywords

biochemistry; bioinformatics; catalysis; enzymes; genetics; molecular biophysics; Chaetomium cupreum; Chi46 protein; PCR; Trichoderma harzianum; amino acid sequence; bioinformatics; cDNA; catalytic domain; endochitinase; glycosyl-hydrolase-18; molecular cloning; sequence analysis; substrate binding; Amino acids; Bioinformatics; Cloning; DNA; Databases; Degradation; Proteins; Chaetomium cupreum; Chitinase; Molecular cloning; Sequence analysis;

fLanguage

English

Publisher

ieee

Conference_Titel

Biomedical Engineering and Informatics (BMEI), 2010 3rd International Conference on

Conference_Location

Yantai

Print_ISBN

978-1-4244-6495-1

Type

conf

DOI

10.1109/BMEI.2010.5639736

Filename

5639736