Related Experiment Video
Updated: Aug 28, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Effects of Protein Functionality on Myofibril Protein-Saccharide Graft Reaction
Tae-Kyung Kim1, Hae In Yong2, Ji Yoon Cha1
1Research Group of Food Processing, Korea Food Research Institute, Wanju 55365, Korea.
Abstract:
The myofibril protein (MP) isolate-saccharide graft reactions was prepared using the Maillard reaction with saccharides. The effects of various saccharides on protein functionality and quality of the Maillard reaction were investigated and compared with those of MP. The grafting degree of the MP isolate-saccharide graft reaction was significantly higher in the reducing sugar-treated groups (lactose, glucose, fructose, and palatinose). The browning intensity of the MP isolate-saccharide graft reaction with fructose, sucrose, and erythitol was higher than that observed in the control reaction (p<0.05). MP that reacted with reducing sugars (glucose, fructose, palatinose, and lactose) had fainter bands than MP that reacted with non-reducing sugars (sucrose, erythitol, trehalose, sorbitol, and xylitol). MPs conjugated with glucose exhibited higher protein solubility. The palatinose and lactose treatments were maximum in water binding capacity, though no significant difference in oil binding capacity among the saccharide treatments was observed. The emulsion stability of the MP isolate-saccharide graft reaction with palatinose and erythitol was higher than that of the control reaction. Therefore, reducing sugars have good protein functionality in the MP isolate-saccharides graft reaction.
More Related Videos
08:34OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
13:53Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
Published on: December 19, 2020
Related Concept Videos
Protein Glycosylation
Glycosylation occurs in...
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
Proteoglycans
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...