Cloning and nucleotide sequence of thebglAgene fromErwinia herbicolaand expression of β-glucosidase activity inEscherichia coli

• DOI: 10.1111/j.1574-6968.1995.tb07512.x
• Publication Date: 2006-01-17T10:07:14Z
• Authors: Laura Marri; Silvia Valentini; Danielle Venditti
• Keywords: 0301 basic medicine; bglA; beta-Glucosidase; Erwinia herbicola; Genetic Vectors; Molecular Sequence Data; Gene Expression Regulation, Enzymologic; β-Glucosidase; 3. Good health; Glycosyl hydrolase family 1; 03 medical and health sciences; Genes, Bacterial; Escherichia coli; Erwinia; β-Glucosidase; bglA; Erwinia herbicola; Glycosyl hydrolase family 1; Cloning, Molecular

Genomic DNA fragments encoding beta-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 beta-glucosidase, expressed in E. coli, showed activity against natural beta-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 beta-glucosidases from glycosyl hydrolase family 1.