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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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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.
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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,...
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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...
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Carbohydrates are essential macronutrients that serve as the body's primary energy source. Their digestion begins in the mouth, where salivary amylase partially breaks down complex carbohydrates such as starch into smaller oligosaccharides. This mechanical and enzymatic activity prepares carbohydrates for further processing in the gastrointestinal tract.
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Prebiotic Effects of α- and β-Galactooligosaccharides: The Structure-Function Relation.

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Summary

Galactooligosaccharides (GOS) have prebiotic effects. This review details GOS structures, their interactions with probiotics like Bifidobacterium and Lactobacillus, and their industrial production.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Food Science

Background:

  • Galactooligosaccharides (GOS) are recognized for their prebiotic properties.
  • GOS exist in two primary forms: raffinose family oligosaccharides (RFO, α-GOS) and lactose-type β-galactooligosaccharides (β-GOS).

Purpose of the Study:

  • To review recent research on GOS structures and their health benefits.
  • To explore the interactions between GOS and probiotics.
  • To examine the genetic basis for GOS synthesis and degradation by probiotic bacteria.

Main Methods:

  • Literature review of recent studies on GOS.
  • Analysis of in vitro and in vivo molecular interactions between GOS and probiotics.
  • Examination of enzymology and genetic factors in GOS metabolism by Bifidobacterium and Lactobacillus.
  • Overview of industrial β-GOS production methods.

Main Results:

  • Probiotic strains, particularly Bifidobacterium and Lactobacillus, exhibit specific preferences for forming and degrading GOS based on length, structure, and linkages.
  • Detailed understanding of GOS structures and their impact on host health.
  • Insights into the enzymatic and genetic mechanisms governing GOS utilization by probiotics.

Conclusions:

  • GOS are significant prebiotics with diverse structures and functions.
  • Probiotic bacteria possess specific GOS metabolism pathways.
  • Industrial production of β-GOS involves various methods with differing efficiencies.