Related Experiment Video

Updated: May 13, 2026

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
13:53

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes

Published on: December 19, 2020

Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation to

J Z Zhong1, Y J Xu, W Liu

  • 1State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China.

Journal of Dairy Science
|March 19, 2013
PubMed

Bovine β-lactoglobulin (β-LG) was conjugated with fructo-oligosaccharides (FOS) by Maillard reaction to investigate the relationship among antigenicity, functional properties, and conformational changes of β-LG. When comparing the antigenicity of β-LG conjugated with FOS at different ratios, the lowest antigenicity of β-LG was observed at a ratio of 1:4, which was about 7 times lower than that of the control β-LG. Thus, the ratio of 1:4 was chosen to conjugate β-LG with FOS, and the functional properties and conformational changes of β-LG-FOS conjugates were investigated. The functional properties (solubility, emulsifying ability, and emulsion stability) of β-LG were enhanced after conjugation with FOS. Furthermore, the molecular weight of β-LG increased from 18.4 to 19.9 kDa after conjugation with FOS, as evaluated by sodium dodecyl sulfate-PAGE and mass spectrometry. Partial unfolding of β-LG occurred after conjugation with FOS, as reflected by the quenching of fluorescence, the red-shift of fluorescence spectra, and the increase of β-strands, which may contribute to the decrease in antigenicity and the improvement of functional properties.

More Related Videos

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Related Concept Videos

Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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...
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...
Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Antigens Involved in Adaptive Immunity01:26

Antigens Involved in Adaptive Immunity

An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.