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<p>The scarcity of siamenoside I (SI) hindered its widespread application. Addressing this challenge, we devised an innovative biocatalytic strategy and biological solution for large-scale SI production. Endo 15, an endophyte from <i>Siraitia grosvenorii</i>, exhibited excellent proficiency in SI synthesis, achieving a remarkable 50.65% SI abundance. By harnessing the extracellular protein of Endo 15 (EP), we further escalated SI abundance to 83.59&#xa0;±&#xa0;2.5%, accompanied by full substrate conversion. Delving into the underlying mechanisms, we identified Exo15, a distinct functional protein derived from EP, displaying merely 48.88% amino acid similarity to the yeast exo-1,3-beta glucanase (Exg1). Successfully overexpressing Exo15 in <i>E. coli</i>, we confirmed its functionality in line with EP. Exo15 exhibited exceptional catalytic prowess, efficiently hydrolyzing mogroside V into the high-potency sweetener SI, with unparalleled activity and specificity. Our groundbreaking approach yielded an impressive SI titer of 54 g/L, coupled with an average conversion rate of 2.5 g/L per hour. These outstanding outcomes underscore the immense potential of Exo15 in cost-effective industrial production of the premium natural sweetener, siamenoside I, paving the way for its widespread adoption.</p>

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Efficient production of the high-intensity natural sweetener siamenoside I by the exo-1,3-beta glucanase (Exo15) from Meyerozyma guilliermondii LHGNSJ-VS01

  • 期刊论文

  • 发表日期：

    2025年3月21日

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  • Hongjiang Wang,
  • Haifeng Xie,
  • Ailing Zhong,
  • Qilin Xie

摘要

The scarcity of siamenoside I (SI) hindered its widespread application. Addressing this challenge, we devised an innovative biocatalytic strategy and biological solution for large-scale SI production. Endo 15, an endophyte from Siraitia grosvenorii, exhibited excellent proficiency in SI synthesis, achieving a remarkable 50.65% SI abundance. By harnessing the extracellular protein of Endo 15 (EP), we further escalated SI abundance to 83.59 ± 2.5%, accompanied by full substrate conversion. Delving into the underlying mechanisms, we identified Exo15, a distinct functional protein derived from EP, displaying merely 48.88% amino acid similarity to the yeast exo-1,3-beta glucanase (Exg1). Successfully overexpressing Exo15 in E. coli, we confirmed its functionality in line with EP. Exo15 exhibited exceptional catalytic prowess, efficiently hydrolyzing mogroside V into the high-potency sweetener SI, with unparalleled activity and specificity. Our groundbreaking approach yielded an impressive SI titer of 54 g/L, coupled with an average conversion rate of 2.5 g/L per hour. These outstanding outcomes underscore the immense potential of Exo15 in cost-effective industrial production of the premium natural sweetener, siamenoside I, paving the way for its widespread adoption.