Cloning, functional expression and characterization of an alkaline protease from Bacillus licheniformis

Ritu Sareen, Uwe T. Bornscheuer, Prashant Mishra

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

A gene (apr 46) encoding a protease was cloned from Bacillus licheniformis RSP-09-37. It had an ORF of 1725 bp, encoding a pre-protein of 575 amino acids (63.2 kDa), 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 55 kDa. 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.

Original languageEnglish
Pages (from-to)1901-1907
Number of pages7
JournalBiotechnology Letters
Volume27
Issue number23-24
DOIs
Publication statusPublished - 01-12-2005

Fingerprint

Cloning
Bacilli
Organism Cloning
Peptide Hydrolases
Amino acids
Amino Acids
Molecular mass
Serine Proteases
Proteins
Escherichia coli
Open Reading Frames
Acetonitrile
Genes
alkaline protease
Bacillus licheniformis

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

Sareen, Ritu ; Bornscheuer, Uwe T. ; Mishra, Prashant. / Cloning, functional expression and characterization of an alkaline protease from Bacillus licheniformis. In: Biotechnology Letters. 2005 ; Vol. 27, No. 23-24. pp. 1901-1907.
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Cloning, functional expression and characterization of an alkaline protease from Bacillus licheniformis. / Sareen, Ritu; Bornscheuer, Uwe T.; Mishra, Prashant.

In: Biotechnology Letters, Vol. 27, No. 23-24, 01.12.2005, p. 1901-1907.

Research output: Contribution to journalArticle

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