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Self-Assembled Pea Protein Isolate Nanoparticles with Various Sizes: Explore the Formation Mechanism

文献类型： 外文期刊

作者： Li, Xiao-Long 1 ; Xie, Qiu-Tao 3 ; Liu, Wen-Jie 1 ; Xu, Bao-Cai 1 ; Zhang, Bao 1 ;

作者机构： 1.Hefei Univ Technol, Engn Res Ctr Bioproc, Minist Educ, Hefei 230009, Anhui, Peoples R China

2.Hefei Univ Technol, Sch Food & Biol Engn, Hefei 230009, Anhui, Peoples R China

3.Hunan Acad Agr Sci, Hunan Agr Prod Proc Inst, Changsha 410082, Peoples R China

关键词： pea protein isolate; potassium metabisulfite; disulfide bond; hydrophobic interactions; nanoparticles

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2021 年 69 卷 34 期

页码：

收录情况： SCI

摘要： Pea protein isolate nanoparticles (PPINs) were successfully prepared by potassium metabisulfite (K2S2O5). The disulfide bonds were disrupted by K2S2O5, and then the PPINs were formed through self-assembly. The average diameter of PPINs increased from 124.7 to 297.5 nm as the concentration of K2S2O5 was increased from 2 to 8 mM, and the PPINs showed higher zeta-potentials (-32.2 to -35.8 mV) and unimodal distribution. The content of free sulfhydryl groups first increased and then decreased with the fracture and reformation of disulfide bonds. Subsequently, the increase of the beta-sheet, which has considerable hydrophobicity, promoted the formation of PPINs. The formation mechanism of PPINs was explored by dissociation tests: hydrophobic interactions maintained the basic skeleton of PPINs, disulfide bonds stabilized the internal structure, and hydrogen bonds existed on the exterior of the particles. This study provided a simple and economical method to fabricate nanoparticles.

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