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Efficient d-Galactose Conversion and Functional Rare Sugar Production via Scaffold-Based Enzyme Complex Platforms.

Su Min Song1, Sung Ok Han2, Jeong Eun Hyeon3

  • 1Department of Next Generation Applied Sciences, Graduate School, Sungshin Women's University, Seoul 01133, Republic of Korea.

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|March 17, 2026
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Summary
This summary is machine-generated.

A novel dual-enzyme cascade using scaffolded enzymes significantly boosts d-sorbose production from d-galactose. This method enhances enzyme efficiency and overcomes limitations in rare sugar biosynthesis for industrial applications.

Keywords:
Catcher–Tag systemD-galactose conversionD-sorbose productionD-tagatoserare sugarsscaffolded enzyme complexes

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Area of Science:

  • Biotechnology and Industrial Microbiology
  • Enzyme Engineering and Biocatalysis
  • Carbohydrate Chemistry and Biosynthesis

Background:

  • d-Sorbose is a valuable rare sugar with increasing demand in food and pharmaceuticals.
  • Conventional enzymatic production methods for d-sorbose suffer from low conversion efficiency and thermodynamic limitations.
  • Efficient biosynthesis of rare sugars is crucial for meeting industrial demands.

Purpose of the Study:

  • To develop an efficient enzymatic cascade for d-sorbose production from d-galactose.
  • To enhance enzyme proximity and cascade efficiency using a scaffold-guided dual-enzyme system.
  • To improve substrate affinity and catalytic efficiency for rare sugar biosynthesis.

Main Methods:

  • Engineered a Catcher-Tag-scaffolded dual-enzyme cascade.
  • Assembled *Lactobacillus* fermentum l-arabinose isomerase (LfAraA) and *Pseudomonas cichorii* d-tagatose 3-epimerase (PcDTEase) onto SpyCatcher/DogCatcher scaffolds.
  • Compared the performance of scaffolded enzymes against free enzymes in the conversion of d-galactose to d-sorbose.

Main Results:

  • The scaffolded dual-enzyme complex significantly enhanced d-sorbose yield by 21% compared to free enzymes.
  • Scaffolded enzymes exhibited improved kinetic parameters, including lower Km and higher kcat/Km.
  • Demonstrated enhanced substrate affinity and catalytic efficiency in the d-galactose to d-sorbose conversion pathway.

Conclusions:

  • Scaffold-guided enzyme assembly provides a robust and scalable platform for rare sugar biosynthesis.
  • This approach effectively overcomes the limitations of conventional enzymatic processes for d-sorbose production.
  • The developed system holds strong potential for industrial application in rare sugar manufacturing.