PEG-modified lipase immobilized onto NH2-MIL-53 MOF for efficient resolution of 4-fluoromandelic acid enantiomers
PEG-modified lipase immobilized onto NH2-MIL-53 MOF for efficient resolution of 4-fluoromandelic acid enantiomers
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PEG 修饰的脂肪酶固定在 NH2-MIL-53 MOF 上，可有效拆分 4-氟扁桃酸对映体
DOI：
10.1016/j.ijbiomac.2020.10.076
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发表时间：
2020
影响因子：
8.2
通讯作者：
唐课文
中科院分区：
文献类型：
--
作者：
袁欣;欧剑;张盼良;许卫风;江笔辉;唐课文
采用共价交联的方法，将荧光假单胞菌（PFL）脂肪酶固定在金属有机骨架（MOF） NH2-MIL-53（Fe）上，制备了一种新型非均相生物催化剂。固定化脂肪酶[PEG-PFL@NH2-MIL-53(Fe)]首次应用于4-氟曼陀罗酸（4-FMA）对映体的对映选择性拆分。优化后的固定化PFL在NH2-MIL-53上的负载能力为224.5 mg PFL/g MOF。最佳酶解条件为：温度50℃，VA/4-FMA底物比6:1，固定化脂肪酶负载60 mg，反应时间12 h。实验结果表明，聚乙二醇（PEG）改性和固定化后，PFL的催化活性和热稳定性显著提高。在65℃时，固定化脂肪酶的催化活性保持在初始活性的86.0%。在最优条件下，固定化PFL催化酯交换反应的转化率为49.6%，对映体过剩率为98.0%。此外，固定化脂肪酶在4个循环后仍保持83%的活性，表现出良好的循环稳定性。
A new heterogeneous bio-catalyst was prepared by the immobilization of lipase fromPseudomonas fluorescents(PFL) onto metal-organic frameworks (MOF), NH2-MIL-53(Fe), using covalent cross-linking. The immobilized lipase [PEG-PFL@NH2-MIL-53(Fe)] was firstly applied in enantioselective resolution of 4-fluoromandelic acid (4-FMA) enantiomers. After optimization of the immobilization PFL onto NH2-MIL-53, its loading capacity is 224.5 mg PFL/g MOF. The optimal enzymatic conditions are temperature of 50 °C, VA/4-FMA substrate ratio of 6:1, immobilized lipase loading of 60 mg and reaction time of 12 h. Experimental results show that the catalytic activity and thermal stability of PFL are significantly improved by polyethylene glycol (PEG) modification and immobilization. At 65 °C, the catalytic activity of immobilized lipase retains 86.0% of initial activity. Under the optimal conditions, the excellent results were obtained with conversion of 49.6% and enantiomer excess of 98.0% for the immobilized PFL catalyzed transesterification reaction. Furthermore, the immobilized lipase exhibits excellent cycle stability with 83% of its initial activity after four cycle.