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<p>Transesterification reactions are fundamental transformations in organic chemistry, yet performing them in aqueous media is challenging because of the competing hydrolysis reaction. In this study, we describe a mutant of alcohol oxidase from <i>Phanerochaete chrysosporium</i> (<i>Pc</i>AOx-VPN) that also exhibits transesterification activity. Moreover, <i>Pc</i>AOx-VPN displays no detectable hydrolytic activity, owing to its hydrophobic active site, which effectively excludes water. These characteristics make <i>Pc</i>AOx-VPN a promising catalyst for transesterification reactions in aqueous media, a context that is typically compromised by competing hydrolysis.</p>

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Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月30日

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  • Bin Wu,
  • Yunjian Ma,
  • Chenhao Feng,
  • Limei Ren,
  • Chiara Domestici,
  • Yutong Wang,
  • Thomas Hilberath,
  • Ulf Hanefeld,
  • Evgeny A. Pidko,
  • Frank Hollmann,
  • Yonghua Wang

摘要

Transesterification reactions are fundamental transformations in organic chemistry, yet performing them in aqueous media is challenging because of the competing hydrolysis reaction. In this study, we describe a mutant of alcohol oxidase from Phanerochaete chrysosporium (PcAOx-VPN) that also exhibits transesterification activity. Moreover, PcAOx-VPN displays no detectable hydrolytic activity, owing to its hydrophobic active site, which effectively excludes water. These characteristics make PcAOx-VPN a promising catalyst for transesterification reactions in aqueous media, a context that is typically compromised by competing hydrolysis.