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Updated: Sep 8, 2025

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

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ブドウモロコシのタンパク質のグリコシル化製品の製造と機能的特徴

Qian Luo1,2, Yan Cui1,2, Weifan Gao1,2

  • 1College of Food Science and Engineering, Jilin Agricultural University, Changchun, Jilin 130118, China.

Food chemistry: X
|August 20, 2025
PubMed
まとめ

麦タンパク質 (BP) をFagopyrum esculentum polysaccharide (FEP) でグリコシル化することで,ビタミンD3の封じ込めの機能性と安定性が改善されました. この改変により,タンパク質の消化性,粘着性,および胆酸結合性が向上する.

キーワード:
麦のタンパク質乾燥グライコシレーション機能特性ビタミンD3ウェット・グリコシレーション

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Protein Glycosylation01:25

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...
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Oligosaccharide Assembly01:24

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...
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Protein Folding Quality Check in the RER01:29

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...
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