1887

Abstract

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.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-136-8-1567
1990-08-01
2019-10-19
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-136-8-1567
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error