Identification and characterization of a novel ( S)-ketoprofen-specific esterase

A new ( S)-ketoprofen specific esterase (EST-Y29) was identified from a metagenome library from environmental samples, which showed homologies with class C-β lactamase, penicillin binding protein, and other lipases/esterases. In order to investigate the biochemical and biophysical properties, the re...

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Bibliographic Details
Published in:International journal of biological macromolecules 2007-06, Vol.41 (1), p.1-7
Main Authors: Yoon, Sangyoung, Kim, SeungBum, Ryu, Yeonwoo, Kim, T. Doohun
Format: Article
Language:English
Subjects:
( S)-ketoprofen
Amino Acid Sequence
Catalytic Domain - genetics
Chromatography, High Pressure Liquid
Circular Dichroism
Esterases - genetics
Esterases - isolation & purification
Esterases - metabolism
Genomic Library
Hydrogen-Ion Concentration
Ketoprofen - metabolism
Light
Microbial esterase
Molecular Sequence Data
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Scattering, Radiation
Sequence Homology, Amino Acid
Solvents
Stability
Substrate Specificity
Temperature
Thermodynamics
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Summary:A new ( S)-ketoprofen specific esterase (EST-Y29) was identified from a metagenome library from environmental samples, which showed homologies with class C-β lactamase, penicillin binding protein, and other lipases/esterases. In order to investigate the biochemical and biophysical properties, the recombinant protein was overexpressed, purified to homogeneity, and characterized. This EST-Y29 has high catalytic activity against p-nitrophenyl esters of short fatty acids (C 2 and C 4) and α-naphthyl acetate with activation energy of 30.4 kJ/mol. We have further characterized EST-Y29 using high performance liquid chromatography (HPLC), circular dichroism (CD), dynamic light scattering (DLS) and size exclusion chromatography (SEC).
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2006.11.010