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Protein Glycosylation

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...

Oligosaccharide Assembly

Oligosaccharide Assembly

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...

Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

Protein Folding Quality Check in the RER

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

Glycosaminoglycans

Glycosaminoglycans

Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
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Loss of Carboxy Group as CO2: Decarboxylation of Malonic Acid Derivatives

Loss of Carboxy Group as CO₂: Decarboxylation of Malonic Acid Derivatives

Just like β-keto acids—which upon thermal decarboxylation form ketones—β-dicarboxylic acids undergo decarboxylation to generate monocarboxylic acids with the liberation of carbon dioxide.

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Related Experiment Video

Updated: Jul 16, 2026

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

Published on: April 11, 2014

[Transglycosylation of L-ascorbic acid].

A A Markosian, L A Abelian, M O Adamian

Prikladnaia Biokhimiia I Mikrobiologiia

|March 10, 2007

Summary

Cyclodextrin glucanotransferases (CGTase) and maltase enzymes were used for transglycosylation of L-ascorbic acid. Thermophilic CGTases showed the highest efficiency, achieving over 60% transglucosylation.

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Last Updated: Jul 16, 2026

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

Published on: April 11, 2014

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Area of Science:

Biochemistry
Enzymology
Carbohydrate Chemistry

Background:

L-ascorbic acid (Vitamin C) is a vital nutrient with limited stability.
Enzymatic modification offers a route to enhance the stability of L-ascorbic acid.
Cyclodextrin glucanotransferases (CGTase) and maltase are enzymes capable of transferring glycosyl residues.

Purpose of the Study:

To investigate the transglycosylation of L-ascorbic acid using various glycosyl donors.
To compare the efficiency of CGTases from different bacterial sources (mesophilic, thermophilic, halophilic) and maltase from Saccharomyces cerevisiae.
To determine the optimal conditions for enhancing L-ascorbic acid stability through enzymatic modification.

Main Methods:

Enzymatic transglycosylation reactions were performed using L-ascorbic acid as the acceptor.
Glycosyl donors included starch, maltodextrin, gamma-cyclodextrin, and maltose.
Cyclodextrin glucanotransferases (CGTase) from mesophilic, thermophilic, and halophilic bacilli, and maltase from Saccharomyces cerevisiae were utilized.
Reaction products were analyzed to determine the degree of transglucosylation.

Main Results:

Cyclodextrin glucanotransferases (CGTase) and maltase effectively catalyzed the transglycosylation of L-ascorbic acid.
CGTases derived from thermophilic bacilli demonstrated superior efficiency compared to mesophilic and halophilic counterparts.
Transglucosylation degrees exceeding 60% were achieved, indicating significant modification of L-ascorbic acid.

Conclusions:

Thermophilic bacterial cyclodextrin glucanotransferases are highly effective biocatalysts for the synthesis of L-ascorbic acid derivatives.
Enzymatic transglycosylation presents a promising strategy for improving the stability and potentially the bioavailability of L-ascorbic acid.
Further research into optimizing these enzymatic processes could lead to enhanced Vitamin C formulations.