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
作者： Yang, Tao 1 ; Lv, Tian 1 ; Wang, Bo 1 ; Zhang, Yue 1 ; Wang, Pei 3 ; Zhou, Qin 3 ; Jiang, Dong 3 ; Zhang, Ping-ping 2 ; Jiang, Hao 1 ;
作者机构： 1.Northwest A&F Univ, Shaanxi Union Res Ctr Univ & Enterprise Grain Proc, Coll Food Sci & Engn, Yangling 712100, Peoples R China
2.Jiangsu Acad Agr Sci, Inst Food Crops, Nanjing 210014, Jiangsu, Peoples R China
3.Nanjing Agr Univ, Coll Agr, Nanjing 210095, Jiangsu, Peoples R China
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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