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Co-immobilization of Short-Chain Dehydrogenase/Reductase and Glucose Dehydrogenase for the Efficient Production of (±)-Ethyl Mandelate

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Abstract

Derivatives of (±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Therefore, efficient routes for the production of these derivatives are highly desirable. The short-chain dehydrogenase/reductase (SDR) is a biocatalyst that could potentially be applied to the synthesis of (±)-ethyl mandelate; however, this enzyme requires the reduced form of the cofactor nicotine adenine dinucleotide (phosphate) (NAD(P)H), which is expensive. In this study, we developed a co-immobilization strategy to overcome the issue of NADPH demand in the SDR catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 were co-immobilized on silica gel. The properties and the catalytic abilities of this dual-enzyme system were evaluated. A final yield of 1.17 mM (±)-ethyl mandelate was obtained from the catalytic conversion of ethyl benzoylformate, with a conversion rate of ethyl benzoylformate to (S)-(+)-mandelate of 71.86% and in an enantiomeric excess of > 99% after 1.5 h. This system offers an efficient route for the biosynthesis of (±)-ethyl mandelate.

Graphical Abstract

In this study, we developed a co-immobilization strategy to overcome the issue of NADPH demand in the SDR catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 were co-immobilized on silica gel. Results showed that, this dual-system offers an efficient route for the biosynthesis of (±)-ethyl mandelate.

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Acknowledgements

The authors are supported by the National Natural Science Foundation cultivation project of Jining medical university (Grant No. JYP201704), the Supporting Fund for Teachers’ research of Jining Medical University (Grant No. JYFC2018KJ031), the Startup Fund of Jining Medical University (Grant No. 6001/600557001), and the National Natural Science Foundation of China (Grant No. 21376215). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from the one mentioned above. We thank Hayden Peacock, PhD, from Liwen Bianji, Edanz Editing China (http://www.liwenbianji.cn/ac), for editing the English text of a draft of this manuscript.

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  1. Xiang Du and Jun-rui Feng contributed equally to this manuscript.

Authors and Affiliations

  1. School of Biological Science, Jining Medical University, Jining, China

    Xiao-huan Liu, Xiang Du, Jun-rui Feng, Jing Guan & Tao Wang

  2. Department of Chemical and Biological Engineering, Zhejiang University, Hangzhou, China

    Mian-Bin Wu & Jian-ping Lin

  3. College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou, China

    Zhao-hui Zhang

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  1. Xiao-huan Liu
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  2. Xiang Du
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  7. Tao Wang
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Correspondence to Tao Wang or Zhao-hui Zhang.

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Liu, Xh., Du, X., Feng, Jr. et al. Co-immobilization of Short-Chain Dehydrogenase/Reductase and Glucose Dehydrogenase for the Efficient Production of (±)-Ethyl Mandelate. Catal Lett 149, 1710–1720 (2019). https://doi.org/10.1007/s10562-019-02727-5

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