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<p>Organic–inorganic hybrid nanoflowers as novel enzyme immobilization scaffolds have garnered increasing attention due to their high specific surface area and facile preparation conditions. Here, multiple enzyme hybrid nanoflower (GO&amp;HRP-hNF) was obtained by using galactose oxidase (GO) and horseradish peroxidase (HRP) as the inner protein components and copper phosphates as the inorganic agents, which catalyzed the oxidation of 1-tetralol into 1-tetralone. The yield of 1-tetralone obtained from GO&amp;HRP-hNF (49.96 ± 2.8%) was 1.4 times higher than that of the free enzyme system (35.75 ± 1.8%). GO&amp;HRP-hNF displayed comparable kinetic parameters with free GO and remarkably enhanced stability under high temperature. Moreover, GO&amp;HRP-hNF retained 80% of its initial activity even after 30 repeated catalytic cycles, demonstrating its satisfactory reusability. This study provides an avenue for the synthesis of 1-tetralone from 1-tetralol by using immobilized multi-enzyme composites in industrial applications.</p> Graphical Abstract <p></p>

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Galactose Oxidase and Horseradish Peroxidase Hybrid Nanoflowers for Biosynthesis of 1-Tetralone

  • 期刊论文

  • 发表日期：

    2025年7月8日

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  • Hui Wang,
  • Ruichen Gao,
  • Wenxia Liu,
  • Jun Xiong,
  • Wen-Yong Lou,
  • Xiaoling Wu

摘要

Organic–inorganic hybrid nanoflowers as novel enzyme immobilization scaffolds have garnered increasing attention due to their high specific surface area and facile preparation conditions. Here, multiple enzyme hybrid nanoflower (GO&HRP-hNF) was obtained by using galactose oxidase (GO) and horseradish peroxidase (HRP) as the inner protein components and copper phosphates as the inorganic agents, which catalyzed the oxidation of 1-tetralol into 1-tetralone. The yield of 1-tetralone obtained from GO&HRP-hNF (49.96 ± 2.8%) was 1.4 times higher than that of the free enzyme system (35.75 ± 1.8%). GO&HRP-hNF displayed comparable kinetic parameters with free GO and remarkably enhanced stability under high temperature. Moreover, GO&HRP-hNF retained 80% of its initial activity even after 30 repeated catalytic cycles, demonstrating its satisfactory reusability. This study provides an avenue for the synthesis of 1-tetralone from 1-tetralol by using immobilized multi-enzyme composites in industrial applications.

Graphical Abstract