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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.
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The mechanism for anionic chain-growth polymerization involves initiation, propagation, and termination steps. In the initiation step, a nucleophilic anion, such as butyl lithium, initiates the polymerization process by attacking the π bond of the vinylic monomer. As a result, a carbanion, stabilized by the electron‐withdrawing group, is generated. The resulting carbanion acts as a Michael donor in the propagation step and attacks the second vinylic monomer, which acts as a Michael...
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Related Experiment Video

Updated: Jul 2, 2025

Activation and Conjugation of Soluble Polysaccharides using 1-Cyano-4-Dimethylaminopyridine Tetrafluoroborate CDAP
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Biocatalytic cascade to polysaccharide amination.

Xuebin Feng1, Siyi Hong1, Hongbo Zhao2

  • 1Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON, M5S 3E5, Canada.

Biotechnology for Biofuels and Bioproducts
|February 26, 2024
PubMed
Summary

This study developed an enzymatic method for polysaccharide amination using oxidase-amine transaminase cascades. Silicibacter pomeroyi amine transaminase (SpATA) showed higher yields and stability, with enzyme engineering improving product outcomes.

Keywords:
Aminated polysaccharideAmine transaminasesEnzymatic cascadeTransaminase activity assay

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High-throughput Synthesis of Carbohydrates and Functionalization of Polyanhydride Nanoparticles
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Area of Science:

  • Biotechnology
  • Enzymology
  • Polymer Chemistry

Background:

  • Chitin is a valuable biopolymer, but its applications are limited by harvesting and structural versatility challenges.
  • A novel two-step cascade reaction using carbohydrate oxidoreductases and amine transaminases was proposed for plant polysaccharide amination.
  • This study focused on comparing two amine transaminases, CvATA and SpATA, and engineering SpATA for improved performance.

Purpose of the Study:

  • To develop a one-pot enzymatic method for polysaccharide amination.
  • To compare the efficiency of CvATA and SpATA in amination reactions.
  • To enhance SpATA activity and stability through enzyme engineering.

Main Methods:

  • Development of a quantitative colorimetric assay for transamination yield measurement.
  • Comparison of CvATA and SpATA performance on various oxidized carbohydrates.
  • Enzyme engineering of SpATA through point mutations.
  • Analysis of aminated carbohydrates using HPLC and XPS, including deuterium labeling.

Main Results:

  • SpATA demonstrated higher operational stability and product yields compared to CvATA.
  • Successful amination of oxidized galactomannan was confirmed.
  • Optimized reaction conditions suppressed side product formation.
  • Engineered SpATA mutants, particularly those with alanine substitutions, showed improved product yields.

Conclusions:

  • A fully enzymatic route for polysaccharide amination was established using oxidase-amine transaminase cascades.
  • Low operational stability of amine transaminases, due to PMP cofactor retention issues, limits cascade yield.
  • Future enzyme engineering should focus on improving SpATA's cofactor affinity and operational stability for enhanced process feasibility.