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<p>Multiple enzymatic biotransformation of methanol into ethanolamine via formaldehyde and glycolaldehyde was investigated. After discovery of an amine transaminase (ATA), the transamination reaction was connected to condensation of formaldehyde into glycolaldehyde. The ATA from <i>Silicibacter pomeroyi</i> (SpATA), which showed broad substrate spectrum from C4 to C14 aliphatic aldehydes, was able to catalyze the transamination of glycolaldehyde into ethanolamine. The kinetic studies revealed that K<sub>M</sub>, k<sub>cat</sub>, and k<sub>cat</sub>/K<sub>M</sub> values for glycolaldehyde were 4.3&#xa0;mM, 2.4&#xa0;s<sup>−1</sup>, and 0.56&#xa0;mM<sup>−1</sup>&#xa0;s<sup>−1</sup>, respectively. The cascade transformation of methanol into ethanolamine via formaldehyde and glycolaldehyde by the isolated alcohol oxidase from <i>Hypoxylon</i> sp., glyoxylate carboligase from <i>Escherichia coli</i>, and the recombinant <i>E. coli</i> cells expressing the SpATA led to production of ethanolamine to a bioconversion of 42%. This study will contribute to valorization of C1 chemicals into industrially relevant multi-carbon products.</p>

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Enzyme/whole-cell biotransformation of C1 compounds into ethanolamine by using an amine transaminase from Silicibacter pomeroyi

  • 期刊论文

  • 发表日期：

    2025年3月19日

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  • Hye-Rim Seo,
  • Ji-Min Woo,
  • Hye-Jin Jo,
  • Huijin Cheon,
  • Min-Ju Seo,
  • Soo-Jin Yeom,
  • Jeong-Sun Kim,
  • Jin-Byung Park

摘要

Multiple enzymatic biotransformation of methanol into ethanolamine via formaldehyde and glycolaldehyde was investigated. After discovery of an amine transaminase (ATA), the transamination reaction was connected to condensation of formaldehyde into glycolaldehyde. The ATA from Silicibacter pomeroyi (SpATA), which showed broad substrate spectrum from C4 to C14 aliphatic aldehydes, was able to catalyze the transamination of glycolaldehyde into ethanolamine. The kinetic studies revealed that KM, kcat, and kcat/KM values for glycolaldehyde were 4.3 mM, 2.4 s−1, and 0.56 mM−1 s−1, respectively. The cascade transformation of methanol into ethanolamine via formaldehyde and glycolaldehyde by the isolated alcohol oxidase from Hypoxylon sp., glyoxylate carboligase from Escherichia coli, and the recombinant E. coli cells expressing the SpATA led to production of ethanolamine to a bioconversion of 42%. This study will contribute to valorization of C1 chemicals into industrially relevant multi-carbon products.