Related Experiment Video
Updated: Aug 5, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Chitosan Mitigates Functional Deterioration of Myofibrillar Protein After Chlorogenic Acid-Induced Oxidation:
Junren Zhao1,2, Yugang Ji1, Wenjing Tao1
1School of Biology and Food Engineering, Guangdong University of Petrochemical Technology, Maoming 525000, China.
Abstract:
Chlorogenic acid (CA) exhibits robust lipid antioxidant activity within meat matrices. However, excess CA generates quinones that alter and damage porcine myofibrillar protein (MP). This study investigated the restorative effects of chitosan (CS) on MPs suffering from CA-induced oxidative damage. Three CA concentrations (0, 50, 100 μmol/g protein) and five CS dosages (0.125-1.0 g/g protein) were used to evaluate conformation, turbidity, surface hydrophobicity, solubility, emulsification, rheology, and gel properties. CA-oxidative damage to MP triggered protein unfolding, thiol depletion and aggregation, greatly lowering solubility, emulsifying capacity, viscoelasticity and water retention. CS exerted biphasic effects on turbidity, surface hydrophobicity, tertiary structure, and solubility only under severe CA-induced oxidative modification (100 μmol/g CA): low-to-medium CS aggravated adverse changes, while 1.0 g/g CS partially reversed such damage. For conformational, emulsion and gel parameters, CS consistently alleviated structural disorder caused by CA-induced oxidative damage across all treatments, with 1.0 g/g CS optimally mitigating α-helix loss and uneven emulsion droplets. Significant CA × CS interactions were detected for conformation, turbidity, surface hydrophobicity, solubility, emulsification and rheology (p < 0.001). Gel strength, water-holding capacity and water distribution exhibited non-significant interactions (p > 0.05), revealing independent additive effects of CA and CS on gel networks. Overall, high-dose CS partially ameliorates structural and functional defects of MP caused by CA-induced oxidative damage, which provides theoretical support for the combined application of polyphenols and polysaccharides in meat protein regulation.
Related Concept Videos
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 sequences.
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
