New Insight Into the Structure-Activity Relationship of Sweet-Tasting Proteins: Protein Sector and Its Role for Sweet Properties.

New Insight Into the Structure-Activity Relationship of Sweet-Tasting Proteins: Protein Sector and Its Role for Sweet Properties.
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DOI:
10.3389/fnut.2021.691368
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发表时间:
2021
影响因子:
5
通讯作者:
Liu B
Liu B
中科院分区:
农林科学2区
文献类型:
--
作者:
Zhao X;Wang C;Zheng Y;Liu B

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甜味蛋白是一种具有显着甜味能力的生物大分子,被认为是未来很有前途的糖类替代品。一些甜味蛋白质已被用于食品和饮料中。然而,这些蛋白质的结构和功能关系仍然难以捉摸,其蛋白质工程指南也是有限的。众所周知,甜味蛋白与甜味受体T1R2/T1R3结合并激活,从而产生甜味。甜味蛋白与甜味受体相互作用的“楔形模型”已有报道。在这篇透视文章中,我们揭示了甜味蛋白质中的分子内相互作用力与它们的性质(甜度和稳定性)直接相关。这种分子内相互作用模式被称为“蛋白质部分”,指的是形成物理连接的一小部分残基,这些残基协同影响蛋白质的功能。基于对以往实验数据的分析,我们认为甜味蛋白质的“蛋白质部分”是决定其甜味特性的关键,这对未来的蛋白质工程具有重要的指导意义。
Sweet-tasting protein is a kind of biomacromolecule that has remarkable sweetening power and is regarded as the promising sugar replacer in the future. Some sweet-tasting proteins has been used in foods and beverages. However, the structure and function relationship of these proteins is still elusive, and guidelines for their protein engineering is limited. It is well-known that the sweet-tasting proteins bind to and activate the sweet taste receptor T1R2/T1R3, thus eliciting their sweetness. The “wedge-model” for describing the interaction between sweet-tasting proteins and sweet taste receptor to elucidate their sweetness has been reported. In this perspective article, we revealed that the intramolecular interaction forces in sweet-tasting proteins is directly correlated to their properties (sweetness and stability). This intramolecular interaction pattern, named as “protein sector,” refers to a small subset of residues forming physically connections, which cooperatively affect the function of the proteins. Based on the analysis of previous experimental data, we suggest that “protein sector” of sweet-tasting proteins is pivotal for their sweet properties, which are meaningful guidelines for the future protein engineering.
通过基因突变和蛋白质工程修饰甜味蛋白莫内林的甜度和稳定性。
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