Genomic DNA fragments encoding β-glucosidase activity from the wild-type strain WD4 of Erwinia herbicola were cloned into Escherichia coli. Two clones containing a common fragment encoded a polypeptide of 58 000 Da. Cloned β- glucosidase, expressed in E. coli, showed activity against natural β- glucoside sugars except for cellobiose. An open reading frame of 1442 bp termed bglA was identified by nucleotide sequencing and it coded for a protein of 480 amino acids (M(r) 53 896) which showed significant homology with β-glucosidases from glycosyl hydrolase family.

Marri, L., Valentini, S., & Venditti, D. (1995). Cloning and nucleotide sequence of bgl A gene from Erwinia herbicola and expression of ß-glucosidase activity in Escherichia coli. FEMS MICROBIOLOGY LETTERS, 128(2), 135-138 [10.1016/0378-1097(95)00096-N].

Cloning and nucleotide sequence of bgl A gene from Erwinia herbicola and expression of ß-glucosidase activity in Escherichia coli.

MARRI, LAURA;
1995

Abstract

Genomic DNA fragments encoding β-glucosidase activity from the wild-type strain WD4 of Erwinia herbicola were cloned into Escherichia coli. Two clones containing a common fragment encoded a polypeptide of 58 000 Da. Cloned β- glucosidase, expressed in E. coli, showed activity against natural β- glucoside sugars except for cellobiose. An open reading frame of 1442 bp termed bglA was identified by nucleotide sequencing and it coded for a protein of 480 amino acids (M(r) 53 896) which showed significant homology with β-glucosidases from glycosyl hydrolase family.
Marri, L., Valentini, S., & Venditti, D. (1995). Cloning and nucleotide sequence of bgl A gene from Erwinia herbicola and expression of ß-glucosidase activity in Escherichia coli. FEMS MICROBIOLOGY LETTERS, 128(2), 135-138 [10.1016/0378-1097(95)00096-N].
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/23865
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