食品与发酵工业 >

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

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

研究报告

山羊乳乳清蛋白热聚集对其乳铁蛋白活性影响

  • 薛海燕 ,
  • 谈雅琳 ,
  • 贺宝元 ,
  • 马军 ,
  • 董祁 ,
  • 李晶莹
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  • 1(陕西科技大学 食品科学与工程学院,陕西 西安,710000)
    2(陕西科技大学 轻工科学与工程学院,陕西 西安,710000)
第一作者:博士,教授(通信作者,E-mail:xuehaiyan@sust.edu.cn)

收稿日期: 2025-10-09

  修回日期: 2025-12-17

  网络出版日期: 2026-07-31

基金资助

陕西省重点研发计划项目(2024NC-GJHX-17,2025CY-JJQ-202);陕西省秦创原“科学家+工程师”队伍(2022KXJ-011);榆林市科技计划项目(2024-CXY-153);陕西科技大学大学生创新训练计划项目(S202410708180)

收起

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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摘要

该研究以山羊乳为原料,系统探究了不同热处理对羊乳清蛋白结构、功能及相互作用的影响。结果表明:山羊乳乳清蛋白质变性程度与热处理强度呈正相关,75 ℃/10 min可作为保留蛋白活性的关键阈值。通过多尺度分析发现,随热处理强度增加,体系zeta电位绝对值从20.9 mV降至11 mV,扫描电镜观察显示,蛋白从均匀分布转为片状聚集;圆二色谱分析显示,经100 ℃/120 s处理后蛋白质二级结构中无规卷曲比例增至35.6%,荧光光谱证实三级结构展开导致疏水基团大量暴露,差示扫描量热分析揭示乳铁蛋白(lactoferrin, LF)在121 ℃时发生完全变性。SDS-PAGE结果证实β-乳球蛋白(β-lactoglobulin, β-Lg)通过游离巯基与LF形成二硫键共价交联,从而导致LF活性中心被掩蔽;而α-乳白蛋白(α-lactalbumin, α-La)聚集体虽未与LF直接交联,但可通过空间位阻效应进一步限制其功能自由度。该研究从分子层面揭示了乳清蛋白热聚集物的产生是羊乳LF的热失活因素之一,为高活性羊乳制品的加工工艺优化提供了重要理论依据。

关键词： 山羊乳; 乳铁蛋白; 热处理蛋白互作

本文引用格式

薛海燕 , 谈雅琳 , 贺宝元 , 马军 , 董祁 , 李晶莹 . 山羊乳乳清蛋白热聚集对其乳铁蛋白活性影响[J]. 食品与发酵工业, 2026 , 52(13) : 250 -259 . DOI: 10.13995/j.cnki.11-1802/ts.044766

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

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