Employment of Magnetic Poly(Styrene-co-Triethylene Gycol Dimethacrylate) as an Immobilization Matrix for Lipase G: Application of Hexyl Oleate Synthesis and Kinetic Study

IF 2.3 4区化学 Q3 CHEMISTRY, PHYSICAL Catalysis Letters Pub Date : 2024-10-07 DOI:10.1007/s10562-024-04819-3

Gabrielle P. de Assis, Vinícius S. Silva, Mateus V. C. da Silva, Amanda B. S. Rangel, Leandro G. Aguiar, Larissa de Freitas

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Abstract

This study aimed to synthesize the emollient ester hexyl oleate by enzymatic catalysis using lipase G from Penicillium camemberti immobilized on the magnetic copolymer poly(styrene-co-triethylene glycol dimethacrylate) (STY-TEGDMA-M). For this, an experimental study was carried out on esterification reactions conducted in solvent-free medium, and the collected data were used to construct a mathematical model. The physical properties of the immobilized derivative were evaluated by scanning electron microscopy and Fourier-transform infrared spectroscopy. The results confirmed that lipase G was successfully immobilized onto the support, with a catalytic activity of 564.63 U g⁻¹. The biocatalyst showed optimum performance at 45 °C, reaching 82% conversion after 48 h of reaction. A chromatographic method was used to confirm the formation of hexyl oleate. A thermal stability assay was conducted, showing that the biocatalyst retained 87% of its initial activity after 4 h of incubation at 60 °C. Mathematical modeling was based on the ping-pong bi-bi kinetic mechanism. The best model was selected according to the lowest value of the corrected Akaike information criterion (AIC_C = 124.776). The model revealed equilibrium constant values (K_eq) ranging from 0.87 to 14.57, maximum rates of the forward reaction ranging from 0.088 to 0.090 mol L⁻¹ min⁻¹, and a maximum rate of the reverse reaction of 0.021 mol L⁻¹ min⁻¹.

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利用磁性聚（苯乙烯-三乙烯基羟基二甲基丙烯酸酯）作为脂肪酶 G 的固定化基质：油酸己酯的合成应用和动力学研究

本研究旨在利用固定在磁性共聚物聚（苯乙烯-三乙二醇二甲基丙烯酸酯）（STY-TEGDMA-M）上的卡门贝氏青霉脂肪酶 G，通过酶催化合成油酸己酯润肤剂。为此，对在无溶剂介质中进行的酯化反应进行了实验研究，并利用收集的数据构建了数学模型。通过扫描电子显微镜和傅立叶变换红外光谱对固定化衍生物的物理性质进行了评估。结果证实，脂肪酶 G 成功地被固定在了载体上，其催化活性为 564.63 U g-1。该生物催化剂在 45 °C 时表现出最佳性能，反应 48 小时后转化率达到 82%。色谱法确认了油酸己酯的形成。热稳定性测试表明，生物催化剂在 60 ℃ 温育 4 小时后仍保持了 87% 的初始活性。数学建模基于乒乓生物动力学机制。根据校正后的 Akaike 信息准则（AICC = 124.776）的最低值选出了最佳模型。该模型显示的平衡常数值（Keq）为 0.87 至 14.57，正向反应的最大速率为 0.088 至 0.090 摩尔升/分钟，反向反应的最大速率为 0.021 摩尔升/分钟。

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来源期刊

Catalysis Letters 化学-物理化学

CiteScore

5.70

自引率

3.60%

发文量

327

审稿时长

1 months

期刊介绍： Catalysis Letters aim is the rapid publication of outstanding and high-impact original research articles in catalysis. The scope of the journal covers a broad range of topics in all fields of both applied and theoretical catalysis, including heterogeneous, homogeneous and biocatalysis. The high-quality original research articles published in Catalysis Letters are subject to rigorous peer review. Accepted papers are published online first and subsequently in print issues. All contributions must include a graphical abstract. Manuscripts should be written in English and the responsibility lies with the authors to ensure that they are grammatically and linguistically correct. Authors for whom English is not the working language are encouraged to consider using a professional language-editing service before submitting their manuscripts.