Mechanistic insights into arginine-mediated gluten solubility enhancement and aggregation inhibition across specific subunit and molecular scales

文献类型： 外文期刊

第一作者： Yang, Tao

作者： Yang, Tao;Lv, Tian;Wang, Bo;Zhang, Yue;Jiang, Hao;Zhang, Ping-ping;Wang, Pei;Zhou, Qin;Jiang, Dong

作者机构：

关键词： HMW-GS; Gluten; Arginine; Solubility; Aggregation inhibition

期刊名称：FOOD HYDROCOLLOIDS （ 影响因子：12.4； 五年影响因子：13.3 ）

ISSN： 0268-005X

年卷期： 2025 年 167 卷

页码：

收录情况： SCI

摘要： This study elucidates the mechanisms by which arginine (Arg(+)) inhibits gluten aggregation and enhances solubility, focusing on individual high-molecular-weight glutenin subunit (HMW-GS) using a set of HMW-GS deletion lines. Comparative analyses with Arg(+), guanidine (Gdn(+)), and glycine (Gly) demonstrated increased solubility in HMW-GS deletion lines compared to wild type, particularly under Arg(+) and Gdn(+), following the order for HMW-GS deletion at: Bx7 > By8 > Ax1 > Dy12 > Dx2. Arg (+) enhanced solubility by quenching gluten structure, primarily restructuring hydrogen bonds, weakening hydrophobic interactions, destabilizing beta-sheets, and facilitating beta-turn and beta-sheet transitions, alongside shifts from ggg to the least stable disulfide bond conformation (tgt). Molecular dynamics simulations revealed the heightened sensitivity of Dx2 to Arg(+), driven by guanidino-mediated interactions and local crowding effects. These findings highlight the dominant role of the guanidino group in solubility enhancement, with carboxyl and alkyl groups playing supporting roles.

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