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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Olefin Metathesis Polymerization: Acyclic Diene Metathesis (ADMET)00:53

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Acyclic diene metathesis polymerization or ADMET polymerization involves cross-metathesis of terminal dienes, such as 1,8-nonadiene, to give linear unsaturated polymer and ethylene. As ADMET is a reversible process, the formed ethylene gas must be removed from the reaction mixture to complete the polymerization process.
Similar to cross-metathesis, ADMET also involves the formation of metallacyclobutane intermediate by [2+2] cycloaddition of one of the double bonds of a terminal diene with...
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Updated: Sep 10, 2025

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Protein language model-assisted directed evolution of cyclodextrinase Enables Precision α-O-Oligosaccharide

Ting Nie1, Zhenxin Yan2, Hao Liu3

  • 1State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China; Institute of Key Biological Raw Material, Shanghai Academy of Experimental Medicine, Shanghai 201401, China.

Bioresource Technology
|August 27, 2025
PubMed
Summary

Researchers engineered a cyclodextrinase enzyme for precise alpha-O-oligosaccharide synthesis. This novel glycoside hydrolase system significantly improves yield and specificity, overcoming limitations in current glycobiology methods.

Keywords:
CyclodextrinaseGeneral protein language modelMotif probeMulti-objective optimizationα-O-oligosaccharide

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Area of Science:

  • Glycobiology
  • Enzyme Engineering
  • Carbohydrate Chemistry

Background:

  • Stereoselective synthesis of alpha-O-oligosaccharides is a significant challenge.
  • Existing glycoside hydrolase methods suffer from low specificity and excessive byproducts.

Purpose of the Study:

  • To develop a precise and efficient system for alpha-O-oligosaccharide synthesis.
  • To engineer a glycoside hydrolase with enhanced transglycosylation activity and specificity.

Main Methods:

  • Utilized cyclodextrin as a donor in a glycoside hydrolase system.
  • Identified a Paenibacillus sp. MY03 cyclodextrinase using an extra sugar binding space (ESBS) motif probe.
  • Employed the Pro-PRIME protein language model for enzyme optimization based on minimal beneficial mutation data.

Main Results:

  • Engineered cyclodextrinase exhibited a 12-fold higher transglycosylation-to-hydrolysis (T/H) ratio.
  • Achieved a significant increase in 4-nitrophenyl-α-d-maltoheptaoside (pNP-G7) yield, from 63% to 98%.
  • The engineered enzyme demonstrated broad substrate promiscuity for diverse applications.

Conclusions:

  • The study presents an effective glycoside hydrolase-based system for precise alpha-O-oligosaccharide synthesis.
  • Protein language model-guided enzyme engineering successfully balanced competing catalytic activities, enhancing enzyme performance.
  • The engineered enzyme holds potential for various biotechnological applications in glycobiology.