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Lipase AK from Pseudomonas fluorescens immobilized on metal organic frameworks for efficient biosynthesis of enantiopure (S)− 1-(4-bromophenyl) ethanol
Process Biochemistry ( IF 3.7 ) Pub Date : 2022-11-30 , DOI: 10.1016/j.procbio.2022.11.022
Chenrui Sun , Shuhui Wu , Ying Wu , Bizhu Sun , Panliang Zhang , Kewen Tang

Immobilization of lipase AK from Pseudomonas fluorescens onto a microsphere support constructed by the metal organic framework (MOF) of NH2-Co-MOF was investigated. The loading capacity of 256.9 mg/g (MOF) with an immobilization yield of 72.3% was achieved. The further investigation demonstrated that AK@NH2-Co-MOF was an efficient catalyst in enantiospecific transesterification of 1-(4-bromophenyl) ethanol (BPE) with vinyl acetate, where the expressed activity of (4.028 ± 0.21)× 10−2 mmol/(min·mg AK@NH2-Co-MOF) was 8 times higher than the free lipase. Under the optimum conditions, BPE enantiomers were resolved by AK@NH2-Co-MOF with conversion of 50.42%, enantiomeric excess > 99% for remaining substrate (ees) and enantiomeric excess > 99 % for product (eep). AK@NH2-Co-MOF is recyclable and 51.62 % of the initial conversion was retained after 5 cycles of reuse. NH2-Co-MOF is promising for enzyme immobilization and the prepared AK@NH2-Co-MOF exhibited great potential for efficient biosynthesis of optically pure BPE.



中文翻译:

来自荧光假单胞菌的脂肪酶 AK 固定在金属有机骨架上,用于对映纯 (S)− 1-(4-溴苯基) 乙醇的高效生物合成

研究了将来自荧光假单胞菌的脂肪酶 AK 固定到由 NH 2 -Co-MOF的金属有机骨架 (MOF) 构建的微球载体上。负载量为 256.9 mg/g (MOF),固定化率为 72.3%。进一步研究表明,AK@NH 2 -Co-MOF是1-(4-溴苯基)乙醇(BPE)与乙酸乙烯酯的对映特异性酯交换反应的有效催化剂,其活性为(4.028 ± 0.21)× 10 -2 mmol/(min·mg AK@NH 2 -Co-MOF)比游离脂肪酶高8倍。在最佳条件下,BPE对映异构体被AK@NH 2拆分-Co-MOF,转化率为 50.42%,剩余底物 ( ee s ) 的对映体过量 > 99%,产物 ( ee p ) 的对映体过量 > 99%。AK@NH 2 -Co-MOF 是可回收的,51.62% 的初始转化率在 5 次循环再利用后得以保留。NH 2 -Co-MOF有望用于酶固定化,所制备的AK@NH 2 -Co-MOF在高效生物合成光学纯BPE方面表现出巨大潜力。

更新日期:2022-12-02
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