漆酶催化丁香酸氧化反应：动力学参数的量热法测定。
Laccase catalysed oxidation of syringic acid: calorimetric determination of kinetic parameters.
机构信息
Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
出版信息
Enzyme Microb Technol. 2012 Apr 5;50(4-5):233-7. doi: 10.1016/j.enzmictec.2012.01.005. Epub 2012 Jan 23.
Isothermal titration calorimetry (ITC) was used to study the oxidation of syringic acid by laccases from two different sources: Galerina sp. HC1 and Trametes versicolor. Total molar heat of reaction with both enzymes was similar (230 kJ/mol for Galerina laccase and 233 kJ/mol for Trametes laccase), and was independent of syringic acid concentration. The kinetic parameters of the reaction were calculated from the single injection assay by applying the nonlinear least squares fitting (NLSF) of experimental data to the Michaelis-Menten equation. Higher values for V(max) were obtained with Galerina sp. laccase, whereas K(m) values were comparable for the two enzymes.
采用等温热力学滴定法（ITC）研究了来自两种不同来源的漆酶（Galerina sp. HC1 和 Trametes versicolor）对丁香酸的氧化作用。两种酶的总反应摩尔热（Galerina 漆酶为 230 kJ/mol，Trametes 漆酶为 233 kJ/mol）相似，且与丁香酸浓度无关。通过单次注射分析，应用非线性最小二乘拟合（NLSF）将实验数据拟合到米氏方程，计算出反应的动力学参数。Galerina sp. 漆酶的 Vmax 值较高，而两种酶的 K m 值相当。
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