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New insights into two yeast BDHs from the PDH subfamily as aldehyde reductases in context of detoxification of lignocellulosic aldehyde inhibitors

Abstract

At least 24 aldehyde reductases from Saccharomyces cerevisiae have been characterized and most function in in situ detoxification of lignocellulosic aldehyde inhibitors, but none is classified into the polyol dehydrogenase (PDH) subfamily of the medium-chain dehydrogenase/reductase (MDR) superfamily. This study confirmed that two (2R,3R)-2,3-butanediol dehydrogenases (BDHs) from industrial (denoted Y)/laboratory (denoted B) strains of S. cerevisiae, Bdh1p(Y)/Bdh1p(B) and Bdh2p(Y)/Bdh2p(B), were members of the PDH subfamily with an NAD(P)H binding domain and a catalytic zinc binding domain, and exhibited reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. Especially, the highest enzyme activity towards acetaldehyde by Bdh2p(Y) was 117.95 U/mg with cofactor nicotinamide adenine dinucleotide reduced (NADH). Based on the comparative kinetic property analysis, Bdh2p(Y)/Bdh2p(B) possessed higher specific activity, substrate affinity, and catalytic efficiency towards glycolaldehyde than Bdh1p(Y)/Bdh1p(B). This was speculated to be related to their 49% sequence differences and five nonsynonymous substitutions (Ser41Thr, Glu173Gln, Ile270Leu, Ile316Met, and Gly317Cys) occurred in their conserved NAD(P)H binding domains. Compared with BDHs from a laboratory strain, Bdh1p(Y) and Bdh2p(Y) from an industrial strain displayed five nonsynonymous mutations (Thr12, Asn61, Glu168, Val222, and Ala235) and three nonsynonymous mutations (Ala34, Ile96, and Ala369), respectively. From a first analysis with selected aldehydes, their reductase activities were different from BDHs of laboratory strain, and their catalytic efficiency was higher towards glycolaldehyde and lower towards acetaldehyde. Comparative investigation of kinetic properties of BDHs from S. cerevisiae as aldehyde reductases provides a guideline for their practical applications in in situ detoxification of aldehyde inhibitors during lignocellulose bioconversion.

Key Points

Two yeast BDHs have enzyme activities for reduction of aldehydes.

Overexpression of BDHs slightly improves yeast tolerance to acetaldehyde and glycolaldehyde.

Bdh1p and Bdh2p differ in enzyme kinetic properties.

BDHs from strains with different genetic backgrounds differ in enzyme kinetic properties.

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Acknowledgments

The authors thank James Allen from Liwen Bianji, Edanz Group China for revising this manuscript.

Funding

This work was funded by the Science and Technology Department of Sichuan Province (No. 2020YFH0142), the National Natural Science Foundation of China (No. 31570086), and the Talent Introduction Fund of Sichuan Agricultural University (No. 01426100).

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MGM, XLK, and YDOY conceived and designed research. XLK, YDOY, YPG, QL, and HYW conducted experiments. XLK, YDOY, and YPG analyzed data. YFG, XL, and QC contributed analytical tools. XLK and YDOY wrote the manuscript. MGM, GTA, and EA revised the manuscript. All authors read and approved the manuscript.

Corresponding author

Correspondence to Menggen Ma.

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The authors declare that they have no competing interests.

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This article does not contain any studies with human participants or animals performed by any of the authors.

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Kuang, X., Ouyang, Y., Guo, Y. et al. New insights into two yeast BDHs from the PDH subfamily as aldehyde reductases in context of detoxification of lignocellulosic aldehyde inhibitors. Appl Microbiol Biotechnol 104, 6679–6692 (2020). https://doi.org/10.1007/s00253-020-10722-9

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  • DOI: https://doi.org/10.1007/s00253-020-10722-9

Keywords

  • Aldehyde reductases
  • BDHs
  • Kinetic property
  • Lignocellulosic inhibitors
  • PDH (polyol dehydrogenase) subfamily