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Modulation of protein glutaminase α-helix and disulfide bonds in a sunflower pollen microgel microenvironment: A strategy to enhance enzyme activity and stability

文献类型： 外文期刊

作者： Chen, Shangwen 1 ; Tao, Caiyan 1 ; Huang, Yawen 1 ; Zhao, Ze 2 ; Miao, Song 3 ; Peng, Dengfeng 1 ; Chen, Yashu 1 ; Zhou, Bin 4 ; Deng, Ziyu 1 ; Deng, Qianchun 1 ;

作者机构： 1.Chinese Acad Agr Sci, Oil Crops Res Inst, Key Lab Oilseeds Proc, Minist Agr, Wuhan 430062, Hubei, Peoples R China

2.Wuhan Univ, Hubei Engn Ctr Nat Polymers Based Med Mat, Hubei Key Lab Biomass Resource Chem & Environm Bio, Sch Resource & Environm Sci,Hubei Int Sci & Techno, Wuhan 430072, Hubei, Peoples R China

3.Teagasc Food Res Ctr, Fermoy P61 C996, Cork, Ireland

4.Hubei Univ Technol, Sch Life & Hlth Sci, Wuhan 430068, Hubei, Peoples R China

关键词： Protein glutaminase; Enzyme stabilizing agent; Sunflower pollen microgel; Microenvironment; Stabilization mechanism

期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）

ISSN： 0308-8146

年卷期： 2025 年 480 卷

页码：

收录情况： SCI

摘要： Protein glutaminase (PGase) can improve plant protein solubility, but its activity tends to decline under the influence of external factors. Here, we developed a novel PGase-stabilizing agent (sunflower pollen microgel, SPMG) and investigated the mechanism for its stabilizing effect on PGase. Alkali treatment could regulate the physicochemical microenvironment of SPMG, and its ability to stabilize PGase declined with prolonged treatment time. SPMG increased PGase activity by a maximum of 49.24 %, while enhanced its storage stability by 30.61 %, 21.64 %, and 26.00 % at 4 degrees C, 25 degrees C, and 37 degrees C, respectively. SPMG improved PGase properties through hydrophobic interaction, resulting in the burying of inner hydrophobic groups and enhancement of intermolecular hydrogen bonding, which promoted the alpha-helix content from 23.28 % to 26.19 %. Additionally, these interactions facilitated the sulfhydryl-disulfide bond exchange reaction between PGase molecules, significantly increasing the disulfide bond content by nearly 80 %. This compact structure ultimately enhanced the activity and stability of PGase.

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