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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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Spatially Segregated MOF Bioreactor Enables Versatile Modular Glycoenzyme Assembly for Hierarchical Glycan Library

Jie Zheng1,2, Han Xu2, Bingzhi Li2

  • 1College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, China.

ACS Applied Materials & Interfaces
|March 17, 2023
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Summary

A new method uses compartmentalized MOF particles to immobilize multiple enzymes, improving the efficiency of synthesizing complex glycans. This platform enhances enzyme stability and compatibility for industrial applications in glycan production.

Keywords:
Cascade reactionenzyme immobilizationglycanmetal−organic frameworkssugar nucleotide

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Area of Science:

  • Biotechnology
  • Chemical Synthesis
  • Materials Science

Background:

  • Multienzyme cascades are crucial for *in vitro* glycan synthesis.
  • Challenges include poor enzyme stability and inter-enzyme incompatibility, leading to inefficient pathways.

Purpose of the Study:

  • To develop a universal immobilization platform for assembling multiple glycoenzymes.
  • To overcome limitations of existing multienzyme systems for efficient glycan synthesis.

Main Methods:

  • Developed a "Modular-Enzymes Assembly by Spatial Segregation" (MASS) strategy.
  • Utilized compartmentalized Metal-Organic Framework (MOF) particles for enzyme immobilization.
  • Demonstrated cofactor regeneration and application in high substrate concentration systems.

Main Results:

  • Achieved efficient preparation of glycosyl donors, disaccharides, oligosaccharides, and polysaccharides.
  • Significantly reduced enzyme interference and cross-inhibition through spatial segregation.
  • Successfully applied the platform in a high substrate concentration reaction system.

Conclusions:

  • The robust multienzyme immobilization platform enhances enzymatic glycan synthesis.
  • This approach offers significant potential for the industrial production of complex glycans.
  • The MASS strategy provides a versatile tool for designing efficient enzymatic bioreactors.