关键词: Biodiesel Free lipase Hydroesterification Kinetic model Thermodynamics parameters Biodiesel Free lipase Hydroesterification Kinetic model Thermodynamics parameters Biodiesel Free lipase Hydroesterification Kinetic model Thermodynamics parameters

Mesh : Biofuels Enzymes, Immobilized / metabolism Esterification Esters Fatty Acids Kinetics Lipase / metabolism Methanol Reproducibility of Results Thermodynamics

来  源:   DOI:10.1016/j.biortech.2022.127335

Abstract:
Eversa® Transform 2.0 lipase used as biocatalyst to biodiesel (fatty acid methyl esters - FAME) synthesis has been the target of interesting studies due to its thermostability and cost-effectiveness. In these researches, data about reaction conditions that result in satisfactory yields were investigated. Nevertheless, kinetic and thermodynamic parameters considering this enzyme are scarce. This paper presents an estimation of kinetic and thermodynamic parameters for the Eversa® Transform 2.0-mediated hydroesterification to FAME synthesis. Kinetic studies were performed for different methanol, water and lipase loads in distinct temperatures. Parameters adjusted by the thermodynamic model indicate that the hydrolysis is decisive in the overall hydroesterification reaction rate and the esterification reaction is endothermic (ΔHe = 38.98 kJ/mol). Formation of enzymatic complexes is favored by increasing the temperature, especially the enzyme-methanol inhibition complex. Statistical analysis showed that the model was not overparameterized, and the small confidence interval indicated good reliability of the estimated parameters.
摘要:
Eversa®Transform2.0脂肪酶用作生物柴油(脂肪酸甲酯-FAME)合成的生物催化剂,由于其热稳定性和成本效益,已成为有趣的研究目标。在这些研究中,研究了有关导致令人满意的产率的反应条件的数据。然而,动力学和热力学参数考虑这种酶是稀缺的。本文介绍了Eversa®Transform2.0介导的加氢酯化到FAME合成的动力学和热力学参数的估计。对不同的甲醇进行了动力学研究,水和脂肪酶负荷在不同的温度。通过热力学模型调整的参数表明,水解在整个加氢酯化反应速率中起决定性作用,并且酯化反应是吸热的(ΔHe=38.98kJ/mol)。增加温度有利于酶复合物的形成,特别是酶-甲醇抑制复合物。统计分析表明,该模型没有过度参数化,置信区间小表示估计参数的可靠性好。
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