Tahir Assam Bin, Jiang Bo, Ali Khubaib
State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, China.
State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 214122, China.
Food Res Int. 2024 Dec;198:115332. doi: 10.1016/j.foodres.2024.115332. Epub 2024 Nov 13.
Limited and unclear research exists on the individual capacity of major fractions of pea protein legumin (PL), vicilin (PV) and albumin (PA), which collectively contribute to the structural and functional properties of pea protein. Findings revealed that PV (72.26 ± 2.6 %) and PA (57.42 ± 4.1 %) displayed better solubility compared to PL. PL fraction possessed a complex three-dimensional structure, higher surface hydrophobicity (S), and superior oil-holding-capacity (OHC) contributing to its 4-fold strength (8.58 ± 0.5 N) and structured gel formation. The smaller particle size of PA was also accountable for the comparatively weaker gels and unstable emulsions compared to PL, while PV had the least emulsifying capacity, by non-uniform droplet distribution in CLSM served as proof. PL was found to be responsible for gelation, emulsification, and foaming in pea protein due to structural factors (relative abundance of α-helix and β-sheet). While, the flexible structure of PV, absence of cysteine residues, and disulfide bridges played a role in characteristics like foaming stability. Some protein in PV gel was found loose and did not appear to participate in gelation, hence forming a significantly weaker gel than PL. Despite relatively less S and complex structure, albumin (PA) had a smoother but weaker gel, more consistent and a smaller droplet size distribution in emulsions (compared to PV). Nonetheless, this study aims to fill a forgotten gap by providing baseline knowledge on the individual fractions of pea protein, defining their roles and paving the path for future research focusing on structural and functional properties of pea protein.
关于豌豆蛋白的主要成分豆球蛋白（PL）、豌豆球蛋白（PV）和清蛋白（PA）的个体功能，现有研究有限且不明确，而这些成分共同决定了豌豆蛋白的结构和功能特性。研究结果表明，与PL相比，PV（72.26±2.6%）和PA（57.42±4.1%）具有更好的溶解性。PL组分具有复杂的三维结构、更高的表面疏水性（S）和优异的持油能力（OHC），这有助于其形成4倍强度（8.58±0.5 N）的结构化凝胶。与PL相比，PA较小的粒径也是其凝胶相对较弱且乳液不稳定的原因，而PV的乳化能力最低，共聚焦激光扫描显微镜（CLSM）中液滴分布不均匀可作为证据。由于结构因素（α-螺旋和β-折叠的相对丰度），PL被认为是豌豆蛋白凝胶化、乳化和起泡的原因。同时，PV的柔性结构、不存在半胱氨酸残基和二硫键在起泡稳定性等特性中发挥了作用。发现PV凝胶中的一些蛋白质松散，似乎没有参与凝胶化，因此形成的凝胶比PL明显更弱。尽管清蛋白（PA）的S相对较低且结构复杂，但其凝胶更光滑但更弱，在乳液中的分布更均匀且液滴尺寸更小（与PV相比）。尽管如此，本研究旨在填补这一被遗忘的空白，提供关于豌豆蛋白各个组分的基础知识，明确它们的作用，并为未来专注于豌豆蛋白结构和功能特性的研究铺平道路。
