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根据戊糖乳杆菌NADH氧化酶的稳定性、氧化还原电位和酶促转化对仿生辅因子进行表征

Characterization of Biomimetic Cofactors According to Stability, Redox Potentials, and Enzymatic Conversion by NADH Oxidase from Lactobacillus pentosus.

作者信息

Nowak Claudia, Pick André, Csepei Lénárd-István, Sieber Volker

机构信息

Technical University of Munich, Department of Life Science Engineering, Straubing Center of Science, Schulgasse 16, 94315, Straubing, Germany.

Fraunhofer Institute for Interfacial Engineering and Biotechnology IGB, Bio, Electro and Chemocatalysis BioCat, Straubing Branch, Schulgasse 11a, 94315, Straubing, Germany.

出版信息

Chembiochem. 2017 Oct 5;18(19):1944-1949. doi: 10.1002/cbic.201700258. Epub 2017 Aug 25.

DOI:10.1002/cbic.201700258
PMID:28752634
Abstract

Oxidoreductases are attractive biocatalysts that convert achiral substrates into products of higher value, but they are also for the most part dependent on nicotinamide cofactors. Recently, biomimetic nicotinamide derivatives have received attention as less costly alternatives to natural cofactors. However, recycling of biomimetics is still challenging because there are only limited opportunities. Here, we have characterized various biomimetic cofactors with regard to stability and redox potentials to find the best alternative to natural cofactors. Further, the cofactor spectrum of NADH oxidase from Lactobacillus pentosus (LpNox) could be expanded, and the enzymatic activity was also compared to activities with different small-molecule catalysts. As a result, we succeeded in identifying several strategies for regeneration of oxidized biomimetics.

摘要

氧化还原酶是一种有吸引力的生物催化剂,可将非手性底物转化为更高价值的产物,但在很大程度上它们也依赖于烟酰胺辅因子。最近,仿生烟酰胺衍生物作为天然辅因子成本更低的替代品受到了关注。然而,仿生剂的循环利用仍然具有挑战性,因为机会有限。在这里,我们对各种仿生辅因子的稳定性和氧化还原电位进行了表征,以找到天然辅因子的最佳替代品。此外,戊糖乳杆菌NADH氧化酶(LpNox)的辅因子谱可以扩展,并且还将酶活性与不同小分子催化剂的活性进行了比较。结果,我们成功地确定了几种氧化态仿生剂再生的策略。

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