Cloning and sequencing of beta-1,4-endoglucanase gene (celA) from Pseudomonas sp YD-15

A beta-1,4-endoglucanase gene (celA) from Pseudomonas sp. YD-15 was cloned in Escherichia coli DH5 alpha and its nucleotide sequence determined. The o pen reading frame of celA was 1830 base pairs and the enzyme was composed o f 609 amino acids with a molecular weight of 63 617 Da. The deduced amino a cid sequence and putative active site of CelA had high amino acid homology with family E cellulases. By dot blot analysis, the induction of celA accor ding to carbon sources was determined. The transcripts hybridizing to the i nternal fragment of celA were detected in total RNA isolated from Pseudomon as sp. YD-15 cells grown on avicel and glycerol, but not from cells grown o n glucose and cellobiose.