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Cloning and characterization of cel 8A gene from Rhizobium leguminosarum bv. trifolii 1536 *
Author(s) -
An J.M.,
Lim W.J.,
Hong S.Y.,
Shin E.C.,
Kim E.J.,
Kim Y.K.,
Park S.R.,
Yun H.D.
Publication year - 2004
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.2004.01485.x
Subject(s) - rhizobium leguminosarum , biology , glycosyl , gene , open reading frame , molecular cloning , escherichia coli , cellulase , microbiology and biotechnology , biochemistry , enzyme , rhizobiaceae , genetics , bacteria , gene expression , peptide sequence , symbiosis
Aims: To isolate the cellulase gene from Rhizobium leguminosarum bv. trifolii 1536. Methods and Results: By the shot‐gun method a clone ( cel 8A) harbouring 3·1 kb genomic DNA fragment from R. leguminosarum bv. trifolii 1536 was obtained. The cel 8A gene coded 348 amino acids and it belongs to the glycosyl hydrolase family 8. The molecular mass of Cel8A protein induced from Escherichia coli DH5 α , appeared to be 35 kDa. The optimum pH and optimum temperature was 7·0, and about 30°C for its enzymatic activity respectively. Conclusions: R. leguminosarum bv. trifolii 1536 had cel 8A gene having an open reading frame of 1047 bp coded for the activity of hydrolyzation of carboxymethyl cellulose. Significance and Impact of the Study: The production of celluloytic enzyme by R. leguminosarum bv. trifolii was confirmed, which would play specific roles in rhizobia. Future study should focus on its role in the infection and nodulation phenomena.