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Biocatalysis in organic solvent systems using thermostable enzymes: esterase-catalysed transesterification of Z-L-tyrosine p-nitrophenyl ester

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

Owusu, RK and COWAN, D (1990) Biocatalysis in organic solvent systems using thermostable enzymes: esterase-catalysed transesterification of Z-L-tyrosine p-nitrophenyl ester. Enzyme and Microbial Technology, 12 (5). pp. 374-377. [Journal article]

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URL: http://dx.doi.org/10.1016/0141-0229(90)90167-O

DOI: doi:10.1016/0141-0229(90)90167-O

Abstract

The esterase-catalysed transesterification of N-carbobenzoxy-l-tyrosinep-nitrophenol ester (Z-Tyrp-NPE) with methanol was studied with water: methanol cosolvent and with dry ethyl acetate as solvent. The crude esterase employed was fully thermostable in both solvents at 44°C. At 88°C esterase activity decreased by 90% in water: methanol (10% v/v) and 30% in dry ethyl acetate after 4 h. The initial rate of transesterification was the same order of magnitude, i.e. 1.7 and 0.95 μmol h−1 unit−1 esterase in the two solvents, respectively. However, Z-TyrpNPE solubility was about 50-fold greater in ethyl acetate compared to the water: methanol cosolvent system, accounting for a 50-fold greater quantity of product formed per experiment in ethyl acetate.Keywords: Esterase; thermophilic enzyme; organic solvent catalyses; transesterification

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:16964
Deposited By:Dr Richard Owusu-Apenten
Deposited On:01 Feb 2011 13:23
Last Modified:28 Jan 2014 14:46

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