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<p><span>d</span>-Glucosaminic acid is a valuable amino acid useful in food and medical applications. It is a highly sought after enantiopure molecule important for the synthesis of drugs and glycopeptides. Current enzymatic synthesis pathways to <span>d</span>-glucosaminic acid carry disadvantages such as low product yield and long reaction times. Herein, the Auxiliary Activity 7 chito-oligosaccharide oxidase from <i>Lentinus brumalis</i>, LbChi7A, was shown as a potent biocatalyst capable of efficiently converting <span>d</span>-glucosamine (GlcN) and <i>N</i>-acetyl-<span>d</span>-glucosamine (GlcNAc) to their respective C<sub>1</sub>-acids. The substrate specificity of LbChi7A towards GlcN and GlcNAc enabled the conversion of at least 90% GlcN to <span>d</span>-glucosaminic acid and 100% GlcNAc to <i>N</i>-acetyl-<span>d</span>-glucosaminic acid within 60&#xa0;min. LbChi7A inhibition by the hydrogen peroxide co-product was not detected, even at 860&#xa0;mM. This single enzymatic conversion offers a clean and efficient process to produce industrially relevant glucosaminic acids, including <span>d</span>-glucosaminic acid and <i>N</i>-acetyl-<span>d</span>-glucosaminic acid.</p>

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Oligosaccharide oxidase for the enzymatic synthesis of glucosaminic acids

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年3月17日

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  • Olanrewaju Raji,
  • Thu V. Vuong,
  • Nadia Davoudvandi,
  • Emma R. Master

摘要

d-Glucosaminic acid is a valuable amino acid useful in food and medical applications. It is a highly sought after enantiopure molecule important for the synthesis of drugs and glycopeptides. Current enzymatic synthesis pathways to d-glucosaminic acid carry disadvantages such as low product yield and long reaction times. Herein, the Auxiliary Activity 7 chito-oligosaccharide oxidase from Lentinus brumalis, LbChi7A, was shown as a potent biocatalyst capable of efficiently converting d-glucosamine (GlcN) and N-acetyl-d-glucosamine (GlcNAc) to their respective C1-acids. The substrate specificity of LbChi7A towards GlcN and GlcNAc enabled the conversion of at least 90% GlcN to d-glucosaminic acid and 100% GlcNAc to N-acetyl-d-glucosaminic acid within 60 min. LbChi7A inhibition by the hydrogen peroxide co-product was not detected, even at 860 mM. This single enzymatic conversion offers a clean and efficient process to produce industrially relevant glucosaminic acids, including d-glucosaminic acid and N-acetyl-d-glucosaminic acid.