Biocatalytic Furfuryl Alcohol Production with Ethanol as the Terminal Reductant Using a Single Enzyme

Victor K. Sharma; Kylee J. Cosse; Thomas P. Binder; Jeffrey S. McFarlane; Alan M. Allgeier

doi:10.1021/acssuschemeng.3c01588

Biocatalytic Furfuryl Alcohol Production with Ethanol as the Terminal Reductant Using a Single Enzyme

Victor K. Sharma, Kylee J. Cosse, Thomas P. Binder, Jeffrey S. McFarlane, Alan M. Allgeier

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Traditionally, furfuryl alcohol (FOL) is produced from biomass-derived furfural (FAL) by hydrogenation using metal-based chemocatalysts. It is challenging due to high metal toxicity, high hydrogen partial pressure, and the need for organic solvents. NAD(P)H-dependent yeast alcohol dehydrogenase I (YADH), which offers high atom economy and up to 100% product selectivity at room temperature in an aqueous medium, is used in this study for the biocatalytic production of FOL from FAL using ethanol (EtOH) as the terminal reductant for in situ regeneration of NAD(P)H. Up to 74% FAL conversion was observed at pH 8 with 40 and 160 mM initial FAL and EtOH concentrations, respectively. The conversion was determined to be equilibrium-limited. Circular dichroism spectroscopy and differential scanning fluorimetry studies of YADH show a significant change in the secondary structure upon treatment with increasing concentrations of aldehydes resulting in loss of catalytic activity. Benign reaction conditions support efforts toward sustainable processing, but opportunities for further improvement by increasing product titer and catalyst stability have been identified. This study lays the framework for developing the science and process for alternatives to biomass-derived ethanol.

Original language	English
Pages (from-to)	10767-10775
Number of pages	9
Journal	ACS Sustainable Chemistry and Engineering
Volume	11
Issue number	29
DOIs	https://doi.org/10.1021/acssuschemeng.3c01588
State	Published - Jul 24 2023
Externally published	Yes

Funding

V.S., T.B., and A.M.A. acknowledge funding from the Kansas Corn Commission Award Number 2205, NMR data collection from Sarah Neuenswander, and CD spectra collection from Dr. Ozan Kumru. K.J.C. was supported by NSF-REU grant number 1757953: REU Site Enriching the Undergraduate Research Experience for Native American Students. J.S.M. was supported by The National Institute of General Medical Sciences of the National Institutes of Health under Award Numbers R16GM146714 and RLMGM118990.

Keywords

NAD
alcohol dehydrogenase
cofactor regeneration
ethanol
furfuryl alcohol

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10.1021/acssuschemeng.3c01588

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@article{e333dfec0a6a42c2b0d75e9778eea4d4,

title = "Biocatalytic Furfuryl Alcohol Production with Ethanol as the Terminal Reductant Using a Single Enzyme",

abstract = "Traditionally, furfuryl alcohol (FOL) is produced from biomass-derived furfural (FAL) by hydrogenation using metal-based chemocatalysts. It is challenging due to high metal toxicity, high hydrogen partial pressure, and the need for organic solvents. NAD(P)H-dependent yeast alcohol dehydrogenase I (YADH), which offers high atom economy and up to 100% product selectivity at room temperature in an aqueous medium, is used in this study for the biocatalytic production of FOL from FAL using ethanol (EtOH) as the terminal reductant for in situ regeneration of NAD(P)H. Up to 74% FAL conversion was observed at pH 8 with 40 and 160 mM initial FAL and EtOH concentrations, respectively. The conversion was determined to be equilibrium-limited. Circular dichroism spectroscopy and differential scanning fluorimetry studies of YADH show a significant change in the secondary structure upon treatment with increasing concentrations of aldehydes resulting in loss of catalytic activity. Benign reaction conditions support efforts toward sustainable processing, but opportunities for further improvement by increasing product titer and catalyst stability have been identified. This study lays the framework for developing the science and process for alternatives to biomass-derived ethanol.",

keywords = "NAD, alcohol dehydrogenase, cofactor regeneration, ethanol, furfuryl alcohol",

author = "Sharma, {Victor K.} and Cosse, {Kylee J.} and Binder, {Thomas P.} and McFarlane, {Jeffrey S.} and Allgeier, {Alan M.}",

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doi = "10.1021/acssuschemeng.3c01588",

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AU - Sharma, Victor K.

AU - Cosse, Kylee J.

AU - Binder, Thomas P.

AU - McFarlane, Jeffrey S.

AU - Allgeier, Alan M.

PY - 2023/7/24

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N2 - Traditionally, furfuryl alcohol (FOL) is produced from biomass-derived furfural (FAL) by hydrogenation using metal-based chemocatalysts. It is challenging due to high metal toxicity, high hydrogen partial pressure, and the need for organic solvents. NAD(P)H-dependent yeast alcohol dehydrogenase I (YADH), which offers high atom economy and up to 100% product selectivity at room temperature in an aqueous medium, is used in this study for the biocatalytic production of FOL from FAL using ethanol (EtOH) as the terminal reductant for in situ regeneration of NAD(P)H. Up to 74% FAL conversion was observed at pH 8 with 40 and 160 mM initial FAL and EtOH concentrations, respectively. The conversion was determined to be equilibrium-limited. Circular dichroism spectroscopy and differential scanning fluorimetry studies of YADH show a significant change in the secondary structure upon treatment with increasing concentrations of aldehydes resulting in loss of catalytic activity. Benign reaction conditions support efforts toward sustainable processing, but opportunities for further improvement by increasing product titer and catalyst stability have been identified. This study lays the framework for developing the science and process for alternatives to biomass-derived ethanol.

AB - Traditionally, furfuryl alcohol (FOL) is produced from biomass-derived furfural (FAL) by hydrogenation using metal-based chemocatalysts. It is challenging due to high metal toxicity, high hydrogen partial pressure, and the need for organic solvents. NAD(P)H-dependent yeast alcohol dehydrogenase I (YADH), which offers high atom economy and up to 100% product selectivity at room temperature in an aqueous medium, is used in this study for the biocatalytic production of FOL from FAL using ethanol (EtOH) as the terminal reductant for in situ regeneration of NAD(P)H. Up to 74% FAL conversion was observed at pH 8 with 40 and 160 mM initial FAL and EtOH concentrations, respectively. The conversion was determined to be equilibrium-limited. Circular dichroism spectroscopy and differential scanning fluorimetry studies of YADH show a significant change in the secondary structure upon treatment with increasing concentrations of aldehydes resulting in loss of catalytic activity. Benign reaction conditions support efforts toward sustainable processing, but opportunities for further improvement by increasing product titer and catalyst stability have been identified. This study lays the framework for developing the science and process for alternatives to biomass-derived ethanol.

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Biocatalytic Furfuryl Alcohol Production with Ethanol as the Terminal Reductant Using a Single Enzyme

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