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<p>α-Arbutin is widely recognized as a safe and highly effective skin-whitening agent in cosmetic formulations, owing to its superior tyrosinase inhibition compared to β-arbutin. In this study, a marine-derived sucrose phosphorylase (Suc75290) was engineered using a semi-rational design to enhance its efficiency in α-arbutin biosynthesis. Based on multiple sequence alignment and structural modeling, Arg134, situated within the flexible loop B near the active site, was identified as a crucial residue influencing hydroquinone (HQ) binding. Engineering of the Arg134 site, which had not been explored in previous sucrose phosphorylase studies for α-arbutin production, proved to be an effective strategy. Saturation mutagenesis of Arg134 identified the variant R134K, which exhibited the highest catalytic performance, showing a 62% increase in transglycosylation activity (9 U/mg) compared to the wild-type enzyme (5.6 U/mg). Under optimal bioconversion conditions (350 mM HQ, 1:6 HQ-to-sucrose molar ratio, 20 U/mL enzyme, pH 7.0–7.5, 45&#xa0;°C, 36&#xa0;h), an α-arbutin yield of 52&#xa0;g/L was achieved. The improved activity and yield highlight the potential of the R134K mutant for the industrial-scale production of α-arbutin in cosmetic applications.</p>

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Semi-Rational Design of a Deep-Sea Metagenomic Sucrose Phosphorylase for Enhanced α-Arbutin Biosynthesis

  • 期刊论文

  • 发表日期：

    2026年1月8日

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  • Wei Wang,
  • Yafang Li,
  • Jingjing Sun,
  • Chengcheng Jiang,
  • Jianhua Hao

摘要

α-Arbutin is widely recognized as a safe and highly effective skin-whitening agent in cosmetic formulations, owing to its superior tyrosinase inhibition compared to β-arbutin. In this study, a marine-derived sucrose phosphorylase (Suc75290) was engineered using a semi-rational design to enhance its efficiency in α-arbutin biosynthesis. Based on multiple sequence alignment and structural modeling, Arg134, situated within the flexible loop B near the active site, was identified as a crucial residue influencing hydroquinone (HQ) binding. Engineering of the Arg134 site, which had not been explored in previous sucrose phosphorylase studies for α-arbutin production, proved to be an effective strategy. Saturation mutagenesis of Arg134 identified the variant R134K, which exhibited the highest catalytic performance, showing a 62% increase in transglycosylation activity (9 U/mg) compared to the wild-type enzyme (5.6 U/mg). Under optimal bioconversion conditions (350 mM HQ, 1:6 HQ-to-sucrose molar ratio, 20 U/mL enzyme, pH 7.0–7.5, 45 °C, 36 h), an α-arbutin yield of 52 g/L was achieved. The improved activity and yield highlight the potential of the R134K mutant for the industrial-scale production of α-arbutin in cosmetic applications.