Thermophilic L-fucose isomerase from Thermanaeromonas toyohensis for L-fucose synthesis from L-fuculose

In Jung Kim, Kyoung Heon Kim

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


The beneficial biological properties of L-fucose have extended its commercial application potential in pharmaceutical, cosmetic, and food industries. Enzymatic production of L-fucose with L-fucose isomerase (L-FucI) is considered a selective, green, and efficient strategy. Efficient sugar production requires thermophilic enzymes with increased reaction rate, reduced risk of microbial contamination, and high sugar solubility. No study has evaluated the applicability of thermophilic L-FucI for L-fucose production. In this study, we explored the biochemical properties of a thermostable L-FucI from Thermanaeromonas toyohensis (TtFucI) using L-fuculose as a substrate. The recombinant TtFucI exhibited thermophilicity and optimum activity at 70 °C. The specific activity, Km, and kcat toward L-fuculose were 199.8 U/mg, 33.4 mM, and 901.7 s−1, respectively. Mn2+ ions increased the activity of the enzyme by ∼10 times and enhanced its thermal stability. Our study, on L-fucose synthesis by thermostable L-FucI, suggests the potential application of this enzyme for the industrial production of L-fucose.

Original languageEnglish
Pages (from-to)131-137
Number of pages7
JournalProcess Biochemistry
Publication statusPublished - 2020 Sep


  • L-
  • L-Fucose
  • L-fucose isomerase
  • Thermanaeromonas toyohensis
  • Thermophilic

ASJC Scopus subject areas

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology


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