食品科学 ›› 2026, Vol. 47 ›› Issue (18): 85-92.doi: 10.7506/spkx1002-6630-20260305-039

• 基础研究 • 上一篇    

基于干热法的曲拉源酪蛋白乳糖糖基化改性机理及性能

毛 婷1,马金勇2,卢蔚雯1,康尚云2,都雯玥1,王治业1,*   

  1. (1.甘肃省科学院生物研究所,甘肃省微生物资源开发利用重点实验室,甘肃 兰州 730000;2.甘肃普罗生物科技有限公司,甘肃 酒泉 735000)
  • 发布日期:2026-09-29
  • 基金资助:
    甘肃省科技计划项目区域协同创新发展专项(25CXQF001);甘肃省科学院重点研发成果转化项目(2025ZDYF-06)

Mechanism of Lactose Glycation of Qula Casein and Properties of the Resulting Products under Dry Heating Conditions

MAO Ting, MA Jinyong, LU Weiwen, KANG Shangyun, DU Wenyue, WANG Zhiye   

  1. (1. Key Laboratory of Microbial Resources Exploitation and Application of Gansu Province, Institute of Biology, Gansu Academy of Sciences, Lanzhou 730000, China; 2. Gansu Puluo Biotech Co. Ltd., Jiuquan 735000, China)
  • Published:2026-09-29

摘要: 以曲拉源酪蛋白为底物,乳糖为糖基供体,采用干热法进行糖基化改性,探究糖基化反应对酪蛋白结构与乳化性能的影响,为开发高性能乳化型蛋白配料提供理论依据。通过单因素试验优化工艺,测定产物的接枝度、乳化活性指数(emulsifying activity index,EAI)及乳化稳定性指数(emulsion stability index,ESI)、疏水性,并利用傅里叶变换红外光谱、圆二色光谱及扫描电镜对产物结构进行表征。结果表明:在乳糖与酪蛋白质量比为1∶1、反应温度60 ℃、反应时间6 h的干热体系下,糖基化反应效果较优,接枝度达31.5%,EAI与ESI分别为81.0 m2/g和88.2 min。与未改性酪蛋白相比,表面疏水性降低了21.4%,而EAI增加了37.8%;α-螺旋及β-折叠降低、无规卷曲增加,形貌由致密块状转变为疏松多孔的网状结构,颗粒尺寸减小且分布更均匀。干热法糖基化改性可有效改善曲拉源酪蛋白乳化性能,其作用机制与蛋白质结构去折叠化及两亲性优化密切相关,本研究为曲拉源酪蛋白的高值化利用提供了可行的改性工艺与理论依据。

关键词: 曲拉;酪蛋白;糖基化;乳化性;光谱

Abstract: To provide a theoretical basis for developing high-performance emulsifying protein ingredients, this study investigated the glycation of casein from Qula cheese using lactose as the sugar donor under dry heating conditions and elucidated the impact of glycation on the structure and emulsifying properties of casein. Single-factor experiments were employed to optimize the reaction conditions. The degree of grafting, emulsifying properties, and hydrophobicity of the products were determined. The products were characterized using Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD) spectroscopy, and scanning electron microscopy (SEM). The results indicated that the highest glycation efficiency was achieved at a lactose-to-casein mass ratio of 1:1, a temperature of 60 ℃, and a reaction time of 6 h. Under these conditions, the degree of grafting reached 31.5%, and the emulsifying activity index (EAI) and emulsion stability index (ESI) were 81.0 m2/g and 88.2 min, respectively. Compared with unmodified casein, the surface hydrophobicity of glycated casein decreased by 21.4%, while its EAI significantly increased by 37.8%. Structural analyses revealed a decrease in α-helix and β-sheet contents and an increase in random coil content. After glycation, the compact block-like structure of native casein was transformed into a loose and porous network structure with reduced and more uniformly distributed particle sizes. Dry-heat glycation modification effectively improves the emulsifying properties of casein. The underlying mechanism is closely related to protein unfolding and improved amphiphilicity. This study provides a theoretical foundation for the high-value utilization of casein from Qula cheese.

Key words: Qula; casein; glycation; emulsifying properties; spectroscopy

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