# Effect of Different High-Temperature Heating Methods on the Glycation Reaction and Advanced Glycation Reaction Products of β-Lactoglobulin

## TL;DR

This study compares how different high-temperature heating methods affect the glycation of β-lactoglobulin, a key dairy protein, and finds that superheated steam causes less damage and fewer harmful byproducts.

## Contribution

The study reveals that superheated steam reduces glycation and structural changes in β-lactoglobulin compared to other heating methods.

## Key findings

- Superheated steam causes less glycation and structural unfolding in β-lactoglobulin than hot air or oil bath.
- Superheated steam produces fewer harmful glycation byproducts like 5-hydroxymethylfurfural and melanogenin.
- Lysine residues are the primary sites of glycation in β-lactoglobulin, as shown by mass spectrometry.

## Abstract

β-lactoglobulin (β-Lg), the major whey protein containing nine lysine residues, serves as an ideal model for studying protein glycation and thermal processing safety in dairy products. This study systematically compared three different high-temperature treatment methods, namely superheated steam (SS), hot air (HA), and oil bath (OB), to investigate their effects on the spatial conformation and glycation product formation of proteins in the β-Lg-glucose system. The results show that compared with OB and HA, SS has a lower degree of glycation, lower consumption of free amino groups, and less unfolding of the protein’s three-dimensional structure. It leads to a lower proportion of α-helix transformation into β-sheet and random coil in the protein. SS resulted in the least browning and produced less 5-hydroxymethylfurfural, pentosidine, fluorescent advanced glycation end products, and melanogenin, yet produced the highest amount of Carboxymethyllysine. Mass spectrometry analysis shows that lysine residues were the primary glycation sites. Therefore, this work provides molecular-level insights into how different heating techniques modulate protein glycation and structural stability, supporting the potential of superheated steam as a gentler alternative to control glycation for β-Lg in food thermal processing.