洞察乳制品素的影响,增强蛋白蛋白的热力学和微观功能
Mohamed Salama1, Mostafa Gouda2, Mahmoud Abou-Elsoud3
1Hubei Hongshan Laboratory, College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; Dairy Department, Food Industries and Nutrition Research Institute, National Research Centre, Dokki 12622, Cairo, Egypt.
素 (CN) 的添加显著提高了蛋白蛋白 (EWP) 的热稳定性,并减少了热巴氏杀菌过程中的聚合. 这种蛋白质结合策略增强了工业应用的EWP功能.
科学领域:
- 食品科学 食品科学 食品科学
- 蛋白质化学 蛋白质化学
- 生物化学 生物化学
背景情况:
- 蛋白蛋白 (EWP) 容易在热巴氏杀菌过程中聚合,这是食品工业面临的关键挑战.
- 了解改善蛋白质热稳定的机制对于加工和产品开发至关重要.
研究的目的:
- 研究素 (CN) 增强蛋白蛋白 (EWP) 热稳定的机制.
- 评估EWP-CN结合对蛋白质聚合,分子间力和质性质的影响.
主要方法:
- 对EWP-CN分子间力量和共价键形成的分析.
- 调查二级结构的热行为和微神经病学.
- 在高温下测量度和确定稳定系数.
主要成果:
- 动态热处理显著增强了EWP-CN硫键和疏水性 (p < 0.05).
- 与单独使用EWP相比,EWP-CN复合物 (2:1,v/v) 在90°C下20分钟表现出较低的度 (61.6%) 和更高的稳定性 (78.2%).
- 素 (10毫克/毫升) 减少了EWP聚合颗粒的1.8倍,支持粘度,储存模量和温度计数据.
结论:
- 与素的结合有效地提高了热稳定性,并减少了蛋白蛋白的聚合.
- 这项研究提出了一种新的方法,使用活性稳定剂来提高像EWP这样敏感蛋白质的耐热性.
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