[Characterization and gene cloning of the endoglucanase from Pseudoalteromonas sp. DY3 strain].
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.
Xiong
Peng-Jun
PJ
The Key Laboratory of Marine Biotechnology, The Third Institute of Oceanography, SOA, Xiamen 361005, China.
Wen
Jian-Jun
JJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D002480:Cellulase / Q000235:genetics*; D003001:Cloning, Molecular; D015971:Gene Expression Regulation, Enzymologic; D008969:Molecular Sequence Data; D031161:Pseudoalteromonas / Q000201:enzymology* / Q000235:genetics*; D016415:Sequence Alignment
D001426:Bacterial Proteins; D002480:Cellulase