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用于己二酸环境友好型生物合成的烯酸酯还原酶的烯烃氢化活性。

Alkene hydrogenation activity of enoate reductases for an environmentally benign biosynthesis of adipic acid.

作者信息

Joo Jeong Chan, Khusnutdinova Anna N, Flick Robert, Kim Taeho, Bornscheuer Uwe T, Yakunin Alexander F, Mahadevan Radhakrishnan

机构信息

Center for Bio-based Chemistry , Division of Convergence Chemistry , Korea Research Institute of Chemical Technology , 141 Gajeong-ro, Yuseong-gu , Daejeon 34114 , Republic of Korea . Email:

Department of Chemical Engineering and Applied Chemistry , University of Toronto , 200 College Street , ON M5S 3E5 , Canada . Email:

出版信息

Chem Sci. 2017 Feb 1;8(2):1406-1413. doi: 10.1039/c6sc02842j. Epub 2016 Oct 11.

Abstract

Adipic acid, a precursor for Nylon-6,6 polymer, is one of the most important commodity chemicals, which is currently produced from petroleum. The biosynthesis of adipic acid from glucose still remains challenging due to the absence of biocatalysts required for the hydrogenation of unsaturated six-carbon dicarboxylic acids to adipic acid. Here, we demonstrate the first enzymatic hydrogenation of 2-hexenedioic acid and muconic acid to adipic acid using enoate reductases (ERs). ERs can hydrogenate 2-hexenedioic acid and muconic acid producing adipic acid with a high conversion rate and yield and . Purified ERs exhibit a broad substrate spectrum including aromatic and aliphatic 2-enoates and a significant oxygen tolerance. The discovery of the hydrogenation activity of ERs contributes to an understanding of the catalytic mechanism of these poorly characterized enzymes and enables the environmentally benign biosynthesis of adipic acid and other chemicals from renewable resources.

摘要

己二酸是尼龙-6,6聚合物的前体,是最重要的大宗商品化学品之一,目前由石油生产。由于缺乏将不饱和六碳二羧酸氢化为己二酸所需的生物催化剂,从葡萄糖生物合成己二酸仍然具有挑战性。在这里,我们展示了使用烯酸酯还原酶(ERs)将2-己烯二酸和粘康酸首次酶促氢化为己二酸。ERs可以将2-己烯二酸和粘康酸氢化为己二酸,转化率和产率都很高。纯化的ERs表现出广泛的底物谱,包括芳香族和脂肪族2-烯酸酯,并且具有显著的氧耐受性。ERs氢化活性的发现有助于理解这些特性尚不明确的酶的催化机制,并实现从可再生资源以环境友好的方式生物合成己二酸和其他化学品。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6a94/5460604/42b57fab3a79/c6sc02842j-s1.jpg

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