Characterization and gene cloning of the endoglucanase from Pseudoalteromonas sp. DY3 strain.
- Author:
Peng-Jun XIONG
1
;
Jian-Jun WEN
Author Information
1. The Key Laboratory of Marine Biotechnology, The Third Institute of Oceanography, SOA, Xiamen 361005, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Bacterial Proteins;
genetics;
Cellulase;
genetics;
Cloning, Molecular;
Gene Expression Regulation, Enzymologic;
Molecular Sequence Data;
Pseudoalteromonas;
enzymology;
genetics;
Sequence Alignment
- From:
Chinese Journal of Biotechnology
2004;20(2):233-237
- CountryChina
- Language:Chinese
-
Abstract:
A bacteria strain DY3 with high endoglucanse activity was isolated from deep sea sediment sample ES0109. The 16S rDNA sequence of DY3 exhibits identity of 99% with those of the same genus bacteria Pseudoalteromonas citrea and Pseudoalteromonas elyakovii . The celX gene of DY3 obtained by PCR method is 1479bp in length and encodes a protein of 492 amino acids. The protein encoded by celX gene exhibits 95% sequence identity with endoglucanase CelG from Pseudoalteromonas haloplanktis. There are two modules in the deduced amino acids sequence, a catalytic domain of glycosyl hydrolases family 5 at the N terminal and a carbohydrate binding domain at the C terminal which was linked to catalytic domain by a short linker. The optimal temperature of CelX is 40 degrees C and the optimal pH was between 6 and 7.
