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<p>Salidroside has been widely utilized in the food and cosmetics industries. However, the efficient synthesis of salidroside remains a challenge. In this study, a potential uridine diphosphate-dependent glycosyltransferase (UGT) from <i>Bacillus subtilis</i> 168 (named UGT<sub>BS</sub>) was identified through evolutionary relationship analysis and molecular docking, with findings subsequently validated by experimental verification. The optimal conversion of UGT<sub>BS</sub> for salidroside synthesis reached 98.4% (mol/mol). Additionally, a conversion exceeding 85% (mol/mol) was achieved using the UGT<sub>BS</sub>-<i>At</i>SuSy cascade reaction with tyrosol concentrations ranging from 1 to 10 mM, demonstrating the substrate tolerance of UGT<sub>BS</sub> at high concentrations. Kinetic determination and molecular docking confirmed that the strengthened hydrogen bonds and suitable active center conformation between the enzyme and substrate may account for the efficient synthesis of salidroside. Furthermore, 43.5 mM of salidroside was obtained using a fed-batch cascade reaction strategy. The UGT<sub>BS</sub> identified in this study shows significant potential for salidroside synthesis, and the strategy employed here serves as a reference for the discovery of related enzymes.</p> Graphical abstract <p></p>

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Efficient synthesis of salidroside using mined glycosyltransferase through cascade reaction

  • 期刊论文

  • 发表日期：

    2025年3月27日

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  • Fucheng Zhu,
  • Zixu Yan,
  • Jingli Dai,
  • Juwen Wang,
  • Shiping Huang,
  • Jingbo Ma,
  • Naidong Chen,
  • Yongjun Zang

摘要

Salidroside has been widely utilized in the food and cosmetics industries. However, the efficient synthesis of salidroside remains a challenge. In this study, a potential uridine diphosphate-dependent glycosyltransferase (UGT) from Bacillus subtilis 168 (named UGTBS) was identified through evolutionary relationship analysis and molecular docking, with findings subsequently validated by experimental verification. The optimal conversion of UGTBS for salidroside synthesis reached 98.4% (mol/mol). Additionally, a conversion exceeding 85% (mol/mol) was achieved using the UGTBS-AtSuSy cascade reaction with tyrosol concentrations ranging from 1 to 10 mM, demonstrating the substrate tolerance of UGTBS at high concentrations. Kinetic determination and molecular docking confirmed that the strengthened hydrogen bonds and suitable active center conformation between the enzyme and substrate may account for the efficient synthesis of salidroside. Furthermore, 43.5 mM of salidroside was obtained using a fed-batch cascade reaction strategy. The UGTBS identified in this study shows significant potential for salidroside synthesis, and the strategy employed here serves as a reference for the discovery of related enzymes.

Graphical abstract