Isolation and partial characterization of a novel thermostable carboxylesterase from a thermophilic Bacillus

RK Owusu, D COWAN

Research output: Contribution to journalArticle

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Abstract

High levels of esterase activity were detected in cell extracts from a thermophilic Bacillus. A single esterase, with an apparent molecular weight of 38,000–45,000, was purified 56-fold with 48% recovery. The partially purified esterase was fully active when assayed at 85°C and retained 90% of initial activity after exposure to a temperature of 105°C for 150 min. This enzyme, designated G18A7 esterase, showed a greater thermostability, more alkaline pH optimum (pH 9.5), and lower sensitivity to inhibitors than an esterase from Bacillus stearothermophilus strain NCA 2184, [Matsunaga, A. et al. (1974) Arch. Biochem. Biophys. 160, 504–513]. Nondenaturing polyacrylamide gel electrophoresis of samples from various stages of the purification sequence indicated that the enzyme might be present in the cell either as an aggregate of active monomers or associated with nonenzymic components
LanguageEnglish
Pages158-163
JournalEnzyme and Microbial Technology
Volume13
Issue number2
DOIs
Publication statusPublished - Feb 1991

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Carboxylesterase
Bacilli
Esterases
Bacillus
Geobacillus stearothermophilus
Arches
Enzymes
Cell Extracts
Electrophoresis
Purification
Polyacrylamide Gel Electrophoresis
Monomers
Molecular Weight
Molecular weight
Recovery
Temperature

Cite this

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abstract = "High levels of esterase activity were detected in cell extracts from a thermophilic Bacillus. A single esterase, with an apparent molecular weight of 38,000–45,000, was purified 56-fold with 48{\%} recovery. The partially purified esterase was fully active when assayed at 85°C and retained 90{\%} of initial activity after exposure to a temperature of 105°C for 150 min. This enzyme, designated G18A7 esterase, showed a greater thermostability, more alkaline pH optimum (pH 9.5), and lower sensitivity to inhibitors than an esterase from Bacillus stearothermophilus strain NCA 2184, [Matsunaga, A. et al. (1974) Arch. Biochem. Biophys. 160, 504–513]. Nondenaturing polyacrylamide gel electrophoresis of samples from various stages of the purification sequence indicated that the enzyme might be present in the cell either as an aggregate of active monomers or associated with nonenzymic components",
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Isolation and partial characterization of a novel thermostable carboxylesterase from a thermophilic Bacillus. / Owusu, RK; COWAN, D.

In: Enzyme and Microbial Technology, Vol. 13, No. 2, 02.1991, p. 158-163.

Research output: Contribution to journalArticle

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