佩里拉种子粉蛋白和不同多醇之间的结合相互作用对蛋白质的结构和功能性质的影响
Dan Wang1, He Li1, Tian-Yu Hou1
1School of Chemistry and Chemical Engineering, North University of China, Taiyuan 030051, China.
Food chemistry
|September 4, 2023
概括
这项研究用多醇修改了菜种子粉蛋白 (PSMP),产生了稳定的结合物. 这些新型PSMP-多联体有效地稳定了乳液中的β-胡卜素,显示出对食品应用的希望.
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
- 生物结合的生物结合
背景情况:
- 佩里拉种子粉蛋白 (PSMP) 是一个未充分利用的蛋白质来源.
- 多因其抗氧化特性和蛋白质修饰潜力而闻名.
- 在乳液中稳定敏感的功能成分,如β-胡卜素,仍然是一个挑战.
研究的目的:
- 通过诱导的反应,通过使用各种多来对PSMP进行共价性修改.
- 为了描述产生的PSMP-多联的特征.
- 为了评估这些结合物的有效性作为乳化剂,以稳定β-胡卜素.
主要方法:
- 性诱导PSMP与酸,原卡特丘酸,咖啡酸,阿皮根因和醇的共价修饰.
- 多结合率的量化. 多结合率的量化.
- 用光谱分析 (光) 来评估结构变化.
- 可溶性测量. 可溶性测量.
- 使用PSMP-多烯合物进行β-胡卜素的乳化.
主要成果:
- 证实了PSMP和测试的多醇之间的成功共价结合.
- PSMP-luteolin表现出最高的结合率 (90.89 ± 1.37 毫克/克).
- PSMP-咖啡酸在光度 (Δ13.4 nm) 中显示出显著的蓝色转移,溶解度增加 (从69.6%增加到83.1%).
- 开发的结合物有效地稳定了乳液中的β-胡卜素.
结论:
- 诱导的对应变异是一种有效的方法,可以创建功能性的PSMP-多联体.
- 这些合物表现出增强的特性,如提高溶解性和结合能力.
- 使用PSMP-多联体的新型乳化系统为提供提供和稳定生物活性化合物,特别是β-胡卜素的有希望的方法.
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