Cloning, Functional Expression and Characterization of an Alkaline Protease from Bacilluslicheniformis

A gene (apr 46) encoding a protease was cloned from Bacilluslicheniformis RSP-09-37. It had an ORF of 1725bp, encoding a pre-protein of 575 amino acids (63.2kDa), which was functionally expressed and processed in E.coli JM 109. The mature protein, Apr 46, consists of 500 amino acids with a calculate...

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Bibliographic Details
Published in:Biotechnology letters 2005-12, Vol.27 (23-24), p.1901-1907
Main Authors: Sareen, Ritu, Bornscheuer, Uwe T, Mishra, Prashant
Format: Article
Language:English
Subjects:
Acetonitrile
Amino acids
Biotechnology
Cloning
Encoding
Genes
Mathematical analysis
Protease
Online Access:Get full text
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Summary:A gene (apr 46) encoding a protease was cloned from Bacilluslicheniformis RSP-09-37. It had an ORF of 1725bp, encoding a pre-protein of 575 amino acids (63.2kDa), which was functionally expressed and processed in E.coli JM 109. The mature protein, Apr 46, consists of 500 amino acids with a calculated molecular mass of 55kDa. This protease shows 29-50% homology to known serine proteases and conserved domains. N-terminal sequencing suggests that Apr 46 protease is identical to a B.licheniformis RSP-09-37 protease, which is further supported by a similar stability in acetonitrile.
ISSN:0141-5492
1573-6776
DOI:10.1007/s10529-005-3901-4