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Engineering a cyclic enzymatic cascade for efficient trehalose biosynthesis from maltodextrin substrates.

Qi Liu1, Yangyang Li1, Haidong Huang1

  • 1Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China; Science Center for Future Foods, Ministry of Education, Jiangnan University, Wuxi 214122, China.

Bioresource Technology
|November 5, 2025
PubMed
Summary
This summary is machine-generated.

This study engineered enzymes for improved trehalose (a sugar used in food and medicine) production. A novel enzyme cascade achieved a record 84.31% conversion rate using maltodextrin, enhancing biosynthetic trehalose production.

Keywords:
Catalytic activityMaltodextrin hydrolysisMultienzyme cascadeThermostabilityTrehalose

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Area of Science:

  • Biotechnology
  • Enzyme Engineering
  • Carbohydrate Chemistry

Background:

  • Trehalose is a valuable disaccharide with applications in pharmaceuticals, food, and cosmetics due to its stability and protein-protective qualities.
  • Current industrial trehalose production uses a two-step enzymatic process (maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase) but suffers from low conversion rates and byproduct accumulation.
  • Suboptimal enzyme performance and the generation of non-convertible short-chain maltooligosaccharides limit the efficiency of existing trehalose biosynthetic pathways.

Purpose of the Study:

  • To enhance the thermostability and catalytic efficiency of key enzymes (TreY and TreZ) involved in trehalose biosynthesis using computer-aided enzyme engineering.
  • To identify and integrate a novel enzyme capable of converting accumulated short-chain maltooligosaccharides into usable substrates for the trehalose pathway.
  • To develop a highly efficient, cyclic multienzyme cascade for the cost-effective biosynthetic production of trehalose from low-cost substrates.

Main Methods:

  • Computer-aided enzyme engineering was used to modify maltooligosyltrehalose synthase (TreY) and maltooligosyltrehalose trehalohydrolase (TreZ) from Arthrobacter ramosus.
  • Computational screening identified a 4-α-glucanotransferase (CSMalQ) from Corallococcus sp. EGB with high efficiency in disproportionating short-chain maltooligosaccharides.
  • A cyclic multienzyme cascade was constructed by integrating engineered TreY, TreZ, and the identified CSMalQ, utilizing maltodextrin as the primary substrate.

Main Results:

  • Engineered TreZ mutant T212P showed a 32.3% increase in thermal stability.
  • Engineered TreY mutant M1 demonstrated a 2.97-fold improvement in thermostability and a 0.63-fold increase in catalytic activity.
  • The integrated cyclic multienzyme cascade achieved a trehalose conversion rate of 84.31%, the highest reported to date, by effectively recycling maltooligosaccharides.

Conclusions:

  • Enzyme engineering significantly improved the performance of key enzymes in trehalose biosynthesis.
  • The integration of CSMalQ effectively addressed the issue of short-chain maltooligosaccharide accumulation, enhancing substrate utilization.
  • The developed cyclic multienzyme cascade represents a promising and highly efficient strategy for the industrial biosynthetic production of trehalose.