New Method for Analysis of Enzymatic Reaction : Thermolysin-Catalyzed Synthesis of Aspartame Precursor
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概要
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Aspartame is an artificial sweetener which is 200 times sweeter than sucrose. A precursor of aspartame, N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester (Z-APM) was synthesized and hydrolyzed with thermolysinn in an aqueous monophasic system. Graphical plotting methods and/or nonlinear regression have been used to analyze enzymatic reactons because of the nonlinear enzymatic rate equations. There are, however, problems : the former require accurate measurement of the initial reaction rate and the latter gives no analytical information. The authors proposed a method to solve the nonlinear enzymatic rate equations with respect to the concentration of a product with the Taylor expansion, especially for the reversible Theorell-Chance mechanism (Murakami, Y., Hirata, M., and Hirata A., J. Ferment. Bioeng., 82,246-252,1996). This solutioins, however, is complex for practical use. In this paper, a simplar solution to explain the thermolysin-catalyzed synthesis of Z-APM is obtained. New methods to determine the kinetic parameters, especially for the reversible Theorell-Chance mechanism, based on the approximated solution are proposed. The results calculated using the obtained kinetic parameters can satisfactorily explain the experimental results, which demonstrates the effectiveness of the proposed analysis. We must know the relation between the concentrations of substrates and a product, and accurately evalate of the result obtained using Taylor expansion when we determine the kinetic parameters using our newly developed methods. The methods to determine the kinetic parameters of the reversible Theorell-Chance mechanism described in this paper is, however, expected to be applied to general enzymatic reactons.
- 公益社団法人日本生物工学会の論文
- 1997-01-25
著者
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Murakami Yoshihiko
Department Of Chemical Engineering Waseda University
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Hirata Akira
Department Of Chemical Engineering Waseda University
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