Summary: The cloning, expression and nucleotide sequence of a 3·74 kb DNA segment on pLS215 containing a β-glucosidase gene() from H17c was investigated. The open reading frame (ORF) of 2490 bp encoded a β-glucosidase of 830 amino acid residues with a calculated of 91800. In C600(pLS215) cells the β-glucosidase was localized in the cytoplasm and these cells produced an additional protein with an apparent of approximately 94000. The gene was expressed from its own regulatory region in and a single mRNA initiation point was identified upstream of the ORF and adjacent to a promoter consensus sequence. The primary structure of the β-glucosidase showed > 40% similarity with a domain of 237 amino acids present in the β-glucosidases of and . The β-glucosidase hydrolysed cellobiose to a limited extent, cellotriose to cellobiose and glucose, and cellotetraose and cellopentaose to predominantly glucose.


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