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<p>Carotenoids are essential natural pigments, and ZISO plays a pivotal role in their biosynthesis. This study compares ZISO enzyme activity in <i>Dunaliella salina</i> and <i>Dunaliella bardawil</i> to evaluate their efficiency in synthesizing 9,9′-di-<i>cis</i>-ζ-carotene. Bacterial strains lacking ZISO (ΔDsZISO, ΔDbZISO) and ZDS (ΔDsZDS, ΔDbZDS) were constructed, and HPLC analysis revealed the accumulation of 9,9′-di-<i>cis</i>-ζ-carotene in ΔDbZDS but not in ΔDsZDS, suggesting that DbZISO exhibits higher activity. Molecular docking and kinetic simulations further indicate that DbZISO forms a more stable complex with 9,9′,15-tri-<i>cis</i>-ζ-carotene, with a binding energy lower than that of DsZISO, where the affinity between DbZISO and the substrate is − 13.09 kcal/mol, and the affinity between DsZISO and the substrate is − 12.13 kcal/mol. These results demonstrate that DbZISO is more efficient than DsZISO in catalyzing the isomerization of carotenoid intermediates. This study provides mechanistic insights into ZISO-mediated carotenoid biosynthesis and establishes a foundation for metabolic engineering aimed at enhancing carotenoid production.</p>

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Comparative analysis of ZISO-mediated carotenoid biosynthesis in Dunaliella salina and Dunaliella bardawil

  • 期刊论文

  • 发表日期：

    2025年9月19日

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  • Jia-Yuan Luo,
  • Qian-Xi Zheng,
  • Ibrahim Muazzam Mukhtar,
  • Yu-Chen Xie,
  • Jv-Liang Dai,
  • Ming-Hua Liang,
  • Hao-Hong Chen,
  • Jian-Guo Jiang

摘要

Carotenoids are essential natural pigments, and ZISO plays a pivotal role in their biosynthesis. This study compares ZISO enzyme activity in Dunaliella salina and Dunaliella bardawil to evaluate their efficiency in synthesizing 9,9′-di-cis-ζ-carotene. Bacterial strains lacking ZISO (ΔDsZISO, ΔDbZISO) and ZDS (ΔDsZDS, ΔDbZDS) were constructed, and HPLC analysis revealed the accumulation of 9,9′-di-cis-ζ-carotene in ΔDbZDS but not in ΔDsZDS, suggesting that DbZISO exhibits higher activity. Molecular docking and kinetic simulations further indicate that DbZISO forms a more stable complex with 9,9′,15-tri-cis-ζ-carotene, with a binding energy lower than that of DsZISO, where the affinity between DbZISO and the substrate is − 13.09 kcal/mol, and the affinity between DsZISO and the substrate is − 12.13 kcal/mol. These results demonstrate that DbZISO is more efficient than DsZISO in catalyzing the isomerization of carotenoid intermediates. This study provides mechanistic insights into ZISO-mediated carotenoid biosynthesis and establishes a foundation for metabolic engineering aimed at enhancing carotenoid production.