Cloning and characterization of a bacterial cell-bound type B carboxylesterase from bacillus sp. BP-7

A clone producing halos on tributyrin plates was isolated from a genomic library of Bacillus sp. BP-7. The insert contained an open reading frame that coded for a protein of 487 amino acids with homology to carboxylesterases. The cloned enzyme showed clear preference for esters of short-chain fatty...

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Bibliographic Details
Published in:Current microbiology 2001-04, Vol.42 (4), p.237-240
Main Authors: PRIM, Nuria, PASTOR, F. I, DIAZ, Pilar
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Bacillus
Bacillus - enzymology
Bacillus - genetics
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Base Sequence
Biological and medical sciences
Biotechnology
Carboxylesterase
Carboxylic Ester Hydrolases - chemistry
Carboxylic Ester Hydrolases - genetics
Carboxylic Ester Hydrolases - metabolism
Cloning
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Enzyme Stability
Enzymes
Escherichia coli - enzymology
Escherichia coli - genetics
esterase
Esters
Fundamental and applied biological sciences. Psychology
Genetics
Genome, Bacterial
Genomic Library
Hymecromone - metabolism
Isoelectric Focusing
Lipolysis
Microbiology
Molecular Sequence Data
Nitrophenols - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Sequence Analysis, DNA
Substrate Specificity
tributyrin
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Summary:A clone producing halos on tributyrin plates was isolated from a genomic library of Bacillus sp. BP-7. The insert contained an open reading frame that coded for a protein of 487 amino acids with homology to carboxylesterases. The cloned enzyme showed clear preference for esters of short-chain fatty acids, being classified as an esterase. Maximum activity was found at 45 degrees C and pH 7.5. The enzyme displayed stability in the pH range from 6 to 9.5, and at temperatures from 4 degrees to 45 degrees C. Zymogram analysis of the protein revealed a molecular mass of 53 kDa and a pI of 5.1. The enzyme showed homology to members of the bacterial subclass of type B carboxylesterases, a set of proteins potentially useful for biotechnological applications.
ISSN:0343-8651
1432-0991
DOI:10.1007/s002840110210