Cyclic Continuous Glycation Enhanced Dispersibility of Myofibrillar Protein: Reaction Efficiency and Sites...

Area of Science:

• Food Science
• Protein Chemistry
• Biochemistry

Background:

• Glycation efficiency is often overlooked, leading to increased production costs.
• Myofibrillar protein (MP) modification with glucose can improve its functional properties.

Purpose of the Study:

• To investigate the mechanism and efficiency of cyclic continuous glycation (CCG) for modifying myofibrillar proteins (MP) with glucose.
• To analyze the impact of CCG on the structural, physicochemical, and functional properties of MP-glucose conjugates.

Main Methods:

• Cyclic continuous glycation (CCG) process applied to myofibrillar protein (MP) and glucose.
• Analysis of protein structure unfolding using physicochemical methods.
• Evaluation of physicochemical properties (solubility, dispersibility, thermal stability).
• Proteomics to identify specific glycated sites on MP.

Main Results:

• CCG significantly increased the glycation rate by 65.43% through enhanced exposure of reactive sites and protein unfolding.
• MP-glucose conjugates demonstrated improved solubility, dispersibility, and thermal stability.
• Proteomics identified preferential glycation on myosin heavy chain tails and enhanced modification on the head region, inhibiting head-head interactions.

Conclusions:

• CCG is an effective method to accelerate MP-glucose covalent binding, improving reaction efficiency.
• The study provides a mechanistic understanding of CCG's impact on protein structure and properties.
• Findings offer a theoretical foundation for utilizing CCG in developing novel meat products.