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

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

Owusu, RK and COWAN, D (1991) Isolation and partial characterization of a novel thermostable carboxylesterase from a thermophilic Bacillus. Enzyme and Microbial Technology, 13 (2). pp. 158-163. [Journal article]

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URL: http://dx.doi.org/10.1016/0141-0229(91)90173-8

DOI: doi:10.1016/0141-0229(91)90173-8

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

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Northern Ireland Centre for Food and Health (NICHE)
ID Code:16961
Deposited By:Dr Richard Owusu-Apenten
Deposited On:01 Feb 2011 13:24
Last Modified:28 Jan 2014 14:46

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