在发酵的大豆蛋白分离物中通过梅拉德反应介导的"糖化甲":解凝的结构和口腔处理行为

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...

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...

Carbohydrate digestion and metabolism break down simple and complex carbohydrates from food into saccharides (i.e., sugars) for the body to use as energy. Carbohydrate digestion starts in the mouth during mastication, or chewing. The masticated carbohydrates remain intact in the stomach. Digestion resumes in the duodenum of the small intestine, where pancreatic alpha-amylase and brush border enzymes of the microvilli convert complex carbohydrates to monosaccharides. Finally, the monosaccharides...