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Cloning, functional expression and characterization of an alkaline protease from Bacillus licheniformis.
- Source :
-
Biotechnology letters [Biotechnol Lett] 2005 Dec; Vol. 27 (23-24), pp. 1901-7. - Publication Year :
- 2005
-
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.
- Subjects :
- Acetonitriles pharmacology
Bacillus genetics
Bacterial Proteins isolation & purification
Bacterial Proteins metabolism
Cloning, Molecular
DNA, Bacterial chemistry
DNA, Bacterial genetics
Dose-Response Relationship, Drug
Electrophoresis, Polyacrylamide Gel
Endopeptidases isolation & purification
Endopeptidases metabolism
Enzyme Stability drug effects
Escherichia coli genetics
Gene Expression Regulation, Enzymologic genetics
Genomic Library
Hydrogen-Ion Concentration
Molecular Sequence Data
Phylogeny
Plasmids genetics
Recombinant Proteins chemistry
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Sequence Analysis, DNA
Serine Endopeptidases genetics
Temperature
Transformation, Bacterial
Bacillus enzymology
Bacterial Proteins genetics
Endopeptidases genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0141-5492
- Volume :
- 27
- Issue :
- 23-24
- Database :
- MEDLINE
- Journal :
- Biotechnology letters
- Publication Type :
- Academic Journal
- Accession number :
- 16328988
- Full Text :
- https://doi.org/10.1007/s10529-005-3901-4