4.7 Review

Pecularities and applications of aryl-alcohol oxidases from fungi

期刊

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷 105, 期 10, 页码 4111-4126

出版社

SPRINGER
DOI: 10.1007/s00253-021-11337-4

关键词

Aryl-alcohol oxidase; GMC family; Lignin degradation; Aryl alcohols; Aliphatic allylic alcohols; Biocatalysis; Bio-based precursors; Flavors

资金

  1. Projekt DEAL
  2. Ministry of Innovation, Science and Research of North Rhine-Westphalia, Germany [313/323-400-002 13]

向作者/读者索取更多资源

Aryl-alcohol oxidases have a broad substrate spectrum and potential applications in various fields, making them promising biocatalysts. However, the challenge lies in producing sufficient amounts of these enzymes for larger-scale applications.
Aryl-alcohol oxidases (AAOs) are FAD-containing enzymes that oxidize a broad range of aromatic as well as aliphatic allylic alcohols to aldehydes. Their broad substrate spectrum accompanied by the only need for molecular oxygen as cosubstrate and production of hydrogen peroxide as sole by-product makes these enzymes very promising biocatalysts. AAOs were used in the synthesis of flavors, fragrances, and other high-value-added compounds and building blocks as well as in dye decolorization and pulp biobleaching. Furthermore, AAOs offer a huge potential as efficient suppliers of hydrogen peroxide for peroxidase- and peroxygenase-catalyzed reactions. A prerequisite for application as biocatalysts at larger scale is the production of AAOs in sufficient amounts. Heterologous expression of these predominantly fungal enzymes is, however, quite challenging. This review summarizes different approaches aiming at enhancing heterologous expression of AAOs and gives an update on substrates accepted by these promising enzymes as well as potential fields of their application.

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