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Purification and biochemical characterization of the carbamate hydrolase from Pseudomonas sp. 50432.
- Source :
-
Biotechnology and applied biochemistry [Biotechnol Appl Biochem] 2002 Aug; Vol. 36 (1), pp. 63-70. - Publication Year :
- 2002
-
Abstract
- A soluble carbamate hydrolase that had a wide specificity was purified 2032-fold from Pseudomonas sp. 50432. This was achieved using a combination of anion-exchange, gel-filtration and hydrophobic-interaction- chromatography techniques. Carbamate hydrolase cleaved the ester linkage of the N-methylcarbamates. The native enzyme was a monomer with a molecular mass of 88 kDa. The optimum pH and temperature of the enzyme activity were 8.5 and 37 degrees C respectively. The tested cations or EDTA did not affect the enzyme activity. However, 2-mercaptoethanol reversibly inhibited the enzyme activity. The enzyme showed the K(m) values of 16 and 12 microM for carbofuran and carbaryl respectively. The purified enzyme did not hydrolyse o-nitrophenyl dimethylcarbamate but hydrolysed several N-methylcarbamates and 1-naphthyl acetate.
- Subjects :
- Carboxylic Ester Hydrolases antagonists & inhibitors
Carboxylic Ester Hydrolases biosynthesis
Enzyme Stability
Hydrogen-Ion Concentration
Hydrolysis
Mercaptoethanol pharmacology
Models, Chemical
Molecular Weight
Pseudomonas classification
Sensitivity and Specificity
Temperature
Carbamates chemistry
Carbofuran chemistry
Carboxylic Ester Hydrolases chemistry
Carboxylic Ester Hydrolases isolation & purification
Pseudomonas enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0885-4513
- Volume :
- 36
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biotechnology and applied biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 12149124
- Full Text :
- https://doi.org/10.1042/ba20020026