Immobilization of Alcohol Dehydrogenase, Acetaldehyde Lyase, and NADH Oxidase for Cascade Enzymatic Conversion of Ethanol to Acetoin

Xue-Yong Li, Jia-Ying Huang, Qiang Zhou, Yuan-Yuan Xu, Ponnandy Prabhu and Ye-Wang Zhang
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Xue-Yong Li: School of Pharmacy, Jiangsu University, Zhenjiang 212013, China
Jia-Ying Huang: School of Pharmacy, Jiangsu University, Zhenjiang 212013, China
Qiang Zhou: School of Pharmacy, Jiangsu University, Zhenjiang 212013, China
Yuan-Yuan Xu: School of Pharmacy, Jiangsu University, Zhenjiang 212013, China
Ponnandy Prabhu: Department of Chemical Engineering, University of Michigan, Ann Arbor, MI 48109, USA
Ye-Wang Zhang: School of Pharmacy, Jiangsu University, Zhenjiang 212013, China

Energies, 2022, vol. 15, issue 12, 1-11

Abstract: Acetoin, a four-carbon hydroxyl-keto compound, is used in the food, pharmaceutical, and chemical industries. The cascade enzymatic production is considered a promising and efficient method to produce acetoin. However, the stability and compatibility of the enzymes under the same catalytic conditions are challenges that need to be resolved. In this work, alcohol dehydrogenase, acetaldehyde lyase, and NADH oxidase were selected to work at the same conditions to efficiently convert ethanol into acetoin. These three enzymes were immobilized on epoxy-modified magnetic nanomaterials to obtain highly stable biocatalysts. The stability and the immobilization conditions, including temperature, pH, enzyme–carrier ratio, and immobilization time, were optimized to obtain the immobilized enzymes with a high catalytic activity. The cascade reactions catalyzed by the immobilized enzymes yielded a high conversion of 90%, suggesting that the use of immobilized enzymes is a promising way to produce acetoin.

Keywords: immobilization; NADH oxidase; acetaldehyde lyase; alcohol dehydrogenase; acetoin; cascade enzymatic reactions (search for similar items in EconPapers)
JEL-codes: Q Q0 Q4 Q40 Q41 Q42 Q43 Q47 Q48 Q49 (search for similar items in EconPapers)
Date: 2022
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