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<p>Alginate lyase is widely used in the preparation of alginate oligosaccharides, medicine production, energy conversion, and so on. In this study, we designed truncated mutants of a marine-derived alginate lyase Algl and identified a highly active mutant CD<sub>317</sub> with less degradation when expressed in a yeast host. The enzyme activity of the secretory CD<sub>317</sub> was 1.4-fold higher than that of the parent Algl. It degraded both polyM and polyG but had a stronger preference for polyM. The optimal temperature of Algl and CD<sub>317</sub> was 40&#xa0;°C and 35&#xa0;°C respectively, for which CD<sub>317</sub> showed better temperature tolerance. Additionally, Ca<sup>2+</sup> highly improved the enzyme activity. Fermentation conditions for CD<sub>317</sub> production were optimized as a culture time of 144&#xa0;h, an inoculum of an OD<sub>600nm</sub> of 0.5, and an inducer concentration of 2% (v/v), respectively. Bioreactor fermentation allowed the highest production of 19,500 U/mL, which was 4.6-fold higher than that in a well-plate. These results indicated that the truncated CD<sub>317</sub> showed good potential for industrial use.</p>

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Heterologous Expression and Functional Characterization of a Truncated Marine Alginate Lyase

  • 期刊论文

  • 发表日期：

    2025年10月14日

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  • Qianqian Shao,
  • Chaoying Yao,
  • Xingbin Wang,
  • Bei Han,
  • Qi Liu,
  • Menghao Cai

摘要

Alginate lyase is widely used in the preparation of alginate oligosaccharides, medicine production, energy conversion, and so on. In this study, we designed truncated mutants of a marine-derived alginate lyase Algl and identified a highly active mutant CD317 with less degradation when expressed in a yeast host. The enzyme activity of the secretory CD317 was 1.4-fold higher than that of the parent Algl. It degraded both polyM and polyG but had a stronger preference for polyM. The optimal temperature of Algl and CD317 was 40 °C and 35 °C respectively, for which CD317 showed better temperature tolerance. Additionally, Ca2+ highly improved the enzyme activity. Fermentation conditions for CD317 production were optimized as a culture time of 144 h, an inoculum of an OD600nm of 0.5, and an inducer concentration of 2% (v/v), respectively. Bioreactor fermentation allowed the highest production of 19,500 U/mL, which was 4.6-fold higher than that in a well-plate. These results indicated that the truncated CD317 showed good potential for industrial use.