在 EGCG 酯化反应中，研究了脂肪酶在乙腈中结构稳定性对其催化活性的影响：FTIR 和 MD 模拟。
Effect of structural stability of lipase in acetonitrile on its catalytic activity in EGCG esterification reaction: FTIR and MD simulation.
机构信息
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Guilin Medical University, No.1 Zhiyuan Road, Lingui District, Guilin City, Guangxi 541004, China.
出版信息
Int J Biol Macromol. 2024 Jan;255:128266. doi: 10.1016/j.ijbiomac.2023.128266. Epub 2023 Nov 19.
In this study, (-)-Epigallocatechin-3-O-gallate (EGCG) esterification reaction was catalyzed by Novozym 435, Lipozyme RM, Lipozyme TLIM, and lipase Amano 30SD in acetonitrile. Fourier transform infrared spectroscopy (FTIR) and molecular dynamic (MD) simulations were used to analyze the structural stability of different lipases in acetonitrile and their effect on EGCG esterification reaction. The results showed that conversion rate of EGCG catalyzed by Lipozyme RM was the highest, followed by Lipozyme TLIM. FTIR indicated that the secondary structure of Lipozyme RM was the most stable. MD simulations suggested that whole structural stability of Lipozyme RM in acetonitrile was superior to Novozym 435 and lipase Amano 30SD and similar to Lipozyme TLIM due to their similar conformation, while the active site of Lipozyme RM is more flexible than that of Lipozyme TLIM, which indicated that lipase with stable whole structure and flexible active site may be more conducive to the esterification of EGCG in acetonitrile. This study provided a direction for rapidly screening lipase to synthetize EGCG or other polyphenols esterified derivatives.
在这项研究中，（-）-表没食子儿茶素没食子酸酯（EGCG）酯化反应在乙腈中由 Novozym 435、Lipozyme RM、Lipozyme TLIM 和脂肪酶 Amano 30SD 催化。傅里叶变换红外光谱（FTIR）和分子动力学（MD）模拟用于分析不同脂肪酶在乙腈中的结构稳定性及其对 EGCG 酯化反应的影响。结果表明，Lipozyme RM 催化 EGCG 的转化率最高，其次是 Lipozyme TLIM。FTIR 表明 Lipozyme RM 的二级结构最稳定。MD 模拟表明，由于它们的构象相似，Lipozyme RM 在乙腈中的整体结构稳定性优于 Novozym 435 和脂肪酶 Amano 30SD，与 Lipozyme TLIM 相似，而 Lipozyme RM 的活性位点比 Lipozyme TLIM 更灵活，这表明具有稳定整体结构和灵活活性位点的脂肪酶可能更有利于 EGCG 在乙腈中的酯化反应。这项研究为快速筛选脂肪酶合成 EGCG 或其他多酚酯化衍生物提供了方向。
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