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用不同的方法提取和脱水的麻蛋白分离物的生物活性评估的综合方法:在预测和体外验证中协同作用

Xuan Dong¹, Xuezhi Bi², Siew Young Quek³

¹Food Science, School of Chemical Sciences, The University of Auckland, Auckland 1010, New Zealand.

|October 5, 2024

概括

使用计算和实验室方法识别了麻蛋白分离物 (HPI) 生物活性. 帕帕因水解显示出对二二甲酶-IV (DPP4) 和血管酶转化酶 (ACE) 抑制的高潜力.

科学领域:

食品科学食品科学食品科学
生物化学生物化学
计算生物学计算生物学

背景情况:

麻蛋白分离物 (HPI) 是生物活性的有希望的来源.
调查HPI生物活性需要有效的查和验证方法.

研究的目的:

开发和验证一个集成的工作流程,用于预测和确认HPI中的生物活性.
为了识别特定的HPI具有迪佩基酶-IV (DPP4) 和血管酶转化酶 (ACE) 抑制活性.

主要方法:

在20种酶化13种主要HPI蛋白的in silico选中,以预测生物活性.
使用帕帕因水解剂对预测的DPP4和ACE抑制活性进行体外验证.
在 silico 预测和 in vitro 实验结果之间的相关性分析.

主要成果:

在分析预测了HPI水解的20种潜在生物活性.
帕帕因水解产生了具有最高预测DPP4和ACE抑制潜力的.
在体外测试证实了显著的DPP4 (IC50:0.32-0.42毫克/毫升) 和ACE (IC50:6.8-9.17微克/毫升) 抑制活性.
在预测和验证的抑制活性之间发现了强烈的相关性 (r2 = 0.96).

结论:

一种集成的in silico和in vitro方法可以有效地预测食品蛋白中的生物活性.
HPI是开发具有抗高血压和抗糖尿病功能的功能性食品的宝贵来源.
这个工作流提供了将HPI加工成增值产品的指导.

关键词:

ангиотензин转化酶抑制剂抑制剂生物活性类的生物活性.生物信息学是一种生物信息学.双基酸酶IV抑制剂双基酸酶IV抑制剂酶性水解是一种酶性水解.

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相关概念视频

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...