An Engineered Self-Sufficient Biocatalyst Enables Scalable Production of Linear alpha-Olefins from Carboxylic Acids

An Engineered Self-Sufficient Biocatalyst Enables Scalable Production of Linear alpha-Olefins from Carboxylic Acids
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一种工程化的自给自足生物催化剂能够利用羧酸大规模生产直链 α-烯烃

DOI:
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发表时间:
2018
期刊:
影响因子:
12.9
通讯作者:
Xiqing Wang 王喜庆
Xiqing Wang 王喜庆
中科院分区:
化学1区
文献类型:
--
作者:
Chen Lu 陆晨;Fenglin Shen 沈枫林;Shuaibo Wang 王帅博;Yuyang Wang 王郁杨;Juan Liu 刘娟;Wen-Ju Bai 白文举;Xiqing Wang 王喜庆

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将脱羧酶OleTJE和P450BM3的还原酶结构域融合在一起,产生了一个自给自足的蛋白质OleT-BM3R,它能够在温和的水条件下,以O2为氧化剂,NADPH为电子供体,有效地催化羧酸氧化脱羧成线性α-烯烃(LAOs)。安装在融合蛋白中的兼容电子转移系统不仅消除了对辅助氧化还原伙伴的需要,而且还提高了脱羧反应活性和广泛的底物范围。与基于亚磷酸酯脱氢酶的NADPH再生系统相结合,在低催化剂负载(~ 0.02 mol %)下,该酶催化反应的产物滴度可达2.51 g L−1,体积产率可达209.2 mg L−1 h−1。凭借其稳定性和可扩展性,这种自给自足的生物催化剂为老挝提供了一种自然友好的方式。
Fusing the decarboxylase OleTJE and the reductase domain of P450BM3 creates a self-sufficient protein, OleT-BM3R, which is able to efficiently catalyze oxidative decarboxylation of carboxylic acids into linearα-olefins (LAOs) under mild aqueous conditions using O2 as the oxidant and NADPH as the electron donor. The compatible electron transfer system installed in the fusion protein not only eliminates the need for auxiliary redox partners, but also results in boosted decarboxylation reactivity and broad substrate scope. Coupled with the phosphite dehydrogenasebased NADPH regeneration system, this enzymatic reaction proceeds with improved product titers of up to 2.51 g L−1 and volumetric productivities of up to 209.2 mg L−1 h−1 at low catalyst loadings (∼0.02 mol %). With its stability and scalability, this self-sufficient biocatalyst offers a nature-friendly approach to deliver LAOs.