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<p>Rare monosaccharides are gaining attentions as low‑calorie sweeteners with desirable techno‑functional attributes for food industry. Enzymatic bioproduction offers a sustainable alternative to chemical synthesis, with thermophilic enzymes enabling high‑temperature operation that improves substrate solubility, lowers viscosity, and reduces contamination. This review consolidates sources, substrate scopes, and biochemical properties of key thermophilic catalysts for rare‑monosaccharides manufacture, including ketose 3‑epimerases, L‑arabinose isomerase, D‑lyxose isomerase, L‑rhamnose isomerase, ribose‑5‑phosphate isomerase, L‑fucose isomerase, and auxiliary enzymes, typically active at 50–95&#xa0;°C with half‑lives from hours to weeks. We highlight protein‑engineering advances (directed evolution, semi‑rational, rational design) that improve catalytic efficiency and thermostability, which imultaneously elevates optimal temperature by 5–25&#xa0;°C and extends half‑lives by up-to ~ 60 fold while maintaining or improving <i>k</i><sub>cat</sub>/<i>K</i><sub>m</sub>. We also survey immobilization platforms, including biomacromolecular scaffolds, synthetic polymers, and inorganic supports, that enhance operational stability and recyclability, delivering 3–20 reuse cycles with 20–95% residual activity and enabling shifts from batch to continuous processing. Finally, we discuss the opportunities in artificial intelligence‑assisted novel thermophilic enzymes discovery and design.</p>

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Thermophilic Enzymes in Rare Monosaccharides Production: Sources, Properties, and Biotechnological Advances

  • 期刊论文

  • 发表日期：

    2025年12月17日

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  • Qingqing Zheng,
  • Yanan Wu,
  • Rui Long,
  • Tangli Yang,
  • Dandan Tang,
  • Wei Liu

摘要

Rare monosaccharides are gaining attentions as low‑calorie sweeteners with desirable techno‑functional attributes for food industry. Enzymatic bioproduction offers a sustainable alternative to chemical synthesis, with thermophilic enzymes enabling high‑temperature operation that improves substrate solubility, lowers viscosity, and reduces contamination. This review consolidates sources, substrate scopes, and biochemical properties of key thermophilic catalysts for rare‑monosaccharides manufacture, including ketose 3‑epimerases, L‑arabinose isomerase, D‑lyxose isomerase, L‑rhamnose isomerase, ribose‑5‑phosphate isomerase, L‑fucose isomerase, and auxiliary enzymes, typically active at 50–95 °C with half‑lives from hours to weeks. We highlight protein‑engineering advances (directed evolution, semi‑rational, rational design) that improve catalytic efficiency and thermostability, which imultaneously elevates optimal temperature by 5–25 °C and extends half‑lives by up-to ~ 60 fold while maintaining or improving kcat/Km. We also survey immobilization platforms, including biomacromolecular scaffolds, synthetic polymers, and inorganic supports, that enhance operational stability and recyclability, delivering 3–20 reuse cycles with 20–95% residual activity and enabling shifts from batch to continuous processing. Finally, we discuss the opportunities in artificial intelligence‑assisted novel thermophilic enzymes discovery and design.