Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation
文献类型： 外文期刊
作者： Luo, Lijuan 1 ; Deng, Yuanyuan 1 ; Liu, Guang 1 ; Zhou, Pengfei 1 ; Zhao, Zhihao 1 ; Li, Ping 1 ; Zhang, Mingwei 1 ;
作者机构： 1.Guangdong Acad Agr Sci, Sericultural & Agrifood Res Inst, Key Lab Funct Foods, Minist Agr & Rural Affairs,Guangdong Key Lab Agr P, Guangzhou 510610, Peoples R China
2.Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Peoples R China
3.Food Lab Zhongyuan, Luohe 462300, Peoples R China
关键词： enzymatic deamidation; secondary structure; tertiary structure; solubility; thermal stability
期刊名称：FOODS （ 影响因子：5.2； 五年影响因子：5.5 ）
ISSN：
年卷期： 2023 年 12 卷 22 期
页码：
收录情况： SCI
摘要： The limited solubility and stability of pea proteins hinder their utilization in liquid formulations. In this study, protein glutaminase (PG) was employed to modify pea protein isolates (PPIs) and obtain deamidated PPI with varying degrees of deamidation (DD, 10-25%). The solubility and thermal stability of these deamidated PPI samples were assessed, and a comprehensive analysis, including SDS-PAGE, zeta potential, FTIR, surface hydrophobicity, and intrinsic fluorescence, was conducted to elucidate the mechanism behind the improvement in their functional properties. The results reveal that PG modification greatly enhances the solubility and heat stability of PPI, with the most notable improvements observed at higher DD (>20%). PG modification increases the net charge of PPI, leading to the unfolding and extension of the protein structures, thus exposing more hydrophobic groups. These structural changes are particularly pronounced when DD exceeds 20%. This increased electrostatic repulsion between carboxyl groups would promote protein unfolding, enhancing interactions with water and hindering the aggregation of unfolded protein in the presence of salts at elevated temperatures (supported by high-performance size exclusion chromatography and transmission electron microscopy). Accordingly, PG-mediated deamidation shows promise in enhancing the functional properties of PPI.
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