Food and Fermentation Industries >

2026 , Vol. 52 >Issue 13: 250 - 259

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.044766

Effect of thermal aggregation of goat milk whey proteins on lactoferrin activity

  • XUE Haiyan ,
  • TAN Yalin ,
  • HE Baoyuan ,
  • MA Jun ,
  • DONG Qi ,
  • LI Jingying
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  • 1(College of Food and Biological Engineering, Shaanxi University of Science & Technology, Xi’an 710000, China)
    2(College of Bioresources Chemical and Materials Engineering, Shaanxi University of Science & Technology, Xi’an 710000, China)

Received date: 2025-10-09

  Revised date: 2025-12-17

  Online published: 2026-07-31

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Abstract

This study used goat milk as the raw material to investigate the effects of different heat treatments on the structure, functionality, and interactions of whey proteins.The degree of denaturation increased with the heating intensity.A treatment of 75 ℃ for 10 min served as the critical threshold for maintaining protein activity.Multiscale analyses showed that the absolute zeta potential decreased from 20.9 mV to 11 mV as heating intensity increased.Scanning electron microscopy revealed a transition from uniform distribution to sheet-like aggregation.Circular dichroism indicated that the proportion of random coil structure rose to 35.6% after treatment at 100 ℃ for 120 s.Fluorescence spectroscopy confirmed that unfolding of tertiary structure exposed large numbers of hydrophobic groups.Differential scanning calorimetry demonstrated that lactoferrin(LF) was completely denatured at 121 ℃.SDS-PAGE verified that β-lactoglobulin(β-Lg) formed covalent disulfide crosslinks with LF through free sulfhydryl groups, directly masking the LF active sites.Although α-lactalbumin(α-La) did not directly crosslink with LF, its aggregation further limited LF activity through steric hindrance.These results reveal that formation of whey protein heat aggregates contributes to LF thermal inactivation at the molecular level.This study provides a theoretical basis for optimizing processing conditions of high-activity goat milk products.

Key words： goat milk; lactoferrin; heat-induced protein interactions

Cite this article

XUE Haiyan , TAN Yalin , HE Baoyuan , MA Jun , DONG Qi , LI Jingying . Effect of thermal aggregation of goat milk whey proteins on lactoferrin activity[J]. Food and Fermentation Industries, 2026 , 52(13) : 250 -259 . DOI: 10.13995/j.cnki.11-1802/ts.044766

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