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首页> 外文期刊>Journal of Biotechnology >Mathematical model for aldol addition catalyzed by two D-fructose-6-phosphate aldolases variants overexpressed in E. coli
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Mathematical model for aldol addition catalyzed by two D-fructose-6-phosphate aldolases variants overexpressed in E. coli

机译：在大肠杆菌中过表达的两个D-果糖-6-磷酸醛缩酶变体催化的醛缩酶加成的数学模型

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摘要

Two D-fructose-6-phosphate aldolase variants namely, single variant FSA A129S and double variant FSA A129S/A165G, were used as catalysts in the aldol addition of dihydroxyacetone (DHA) to N-Cbz-3-aminopropanal. Mathematical model for reaction catalyzed by both enzymes, consisting of kinetic and mass balance equations, was developed. Kinetic parameters were estimated from the experimental data gathered by using the initial reaction rate method. The model was validated in the batch and continuously operated ultrafiltration membrane reactor (UFMR). The same type of kinetic model could be applied for both enzymes. The operational stability of the aldolases was assessed by measuring enzyme activity during the experiments. FSA A129S/A165G had better operational stability in the batch reactor (half-life time 26.7 h) in comparison to FSA A129S (half-life time 5.78 h). Both variants were unstable in the continuously operated UFMR in which half-life times were 1.99 and 3.64 h for FSA A129S and FSA A129S/A165G, respectively
机译：在N-Cbz-3-氨基丙醛向二羟丙酮（DHA）的醛醇醛加成中，使用了两种D-果糖6-磷酸醛缩酶醛糖酶变体，即单一变体FSA A129S和双重变体FSA A129S / A165G。建立了由两种酶催化的反应的数学模型，该模型由动力学和质量平衡方程组成。动力学参数是通过使用初始反应速率方法收集的实验数据估算的。该模型在间歇和连续运行的超滤膜反应器（UFMR）中得到验证。两种酶都可以使用相同类型的动力学模型。通过测量实验期间的酶活性来评估醛缩酶的操作稳定性。与FSA A129S（半衰期为5.78小时）相比，FSA A129S / A165G在间歇式反应器中具有更好的运行稳定性（半衰期为26.7小时）。两种变体在连续运行的UFMR中均不稳定，其中FSA A129S和FSA A129S / A165G的半衰期分别为1.99和3.64 h

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