Department of Animal, Veterinary and Food Sciences, University of Idaho, 875 Perimeter Drive, Moscow, ID 83844, United States.
Department of Food Science and Technology, the Ohio State University, 2015 Fyffe Rd, Columbus, OH 43210, United States.
Food Res Int. 2024 Jul;188:114474. doi: 10.1016/j.foodres.2024.114474. Epub 2024 May 10.
Limited proteolysis, CaCl and carboxymethyl cellulose (CMC) have individually demonstrated ability to increase the gel strength of laboratory-extracted plant proteins. However, the syneresis effects of their combination on the gelling capacity of commercial plant protein remains unclear. This was investigated by measuring the rheological property, microstructure and protein-protein interactions of gels formed from Alcalase hydrolyzed or intact pea proteins in the presence of 0.1 % CMC and 0-25 mM CaCl. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed the molecular weight of pea protein in the mixture were < 15 kDa after hydrolysis. The hydrolysates showed higher intrinsic fluorescence intensity and lower surface hydrophobicity than the intact proteins. Rheology showed that the storage modulus (G') of hydrolyzed pea protein (PPH)-based gels sightly decreased compared to those of native proteins. 5-15 mM CaCl increased the G' for both PP and PPH-based gels and decreased the strain in the creep-recovery test. Scanning electron microscopy (SEM) showed the presence of smaller protein aggregates in the PPH-based gels compared to PP gels and the gel network became denser, and more compact and heterogenous in the presence of 15 and 25 mM CaCl. The gel dissociation assay revealed that hydrophobic interactions and hydrogen bonds were the dominant forces to maintain the gel structure. In vitro digestion showed that the soluble protein content in PPH-based gels was 10 ∼ 30 % higher compared to those of the PP counterpart. CaCl addition reduced protein digestibility with a concentration dependent behavior. The results obtained show contrasting effects of limited proteolysis and CaCl on the gelling capacity and digestibility of commercial pea proteins. These findings offer practical guidelines for developing pea protein-based food products with a balanced texture and protein nutrition through formulation and enzymatic pre-treatment.
有限水解、CaCl 和羧甲基纤维素（CMC）已分别证明能够提高实验室提取的植物蛋白的凝胶强度。然而，它们组合对商业植物蛋白凝胶能力的持水收缩效果仍不清楚。本研究通过测量存在 0.1% CMC 和 0-25 mM CaCl 时由 Alcalase 水解或完整豌豆蛋白形成的凝胶的流变特性、微观结构和蛋白质-蛋白质相互作用来研究这一点。十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）显示混合物中豌豆蛋白的分子量<15 kDa，水解后。水解产物的内源荧光强度高于完整蛋白质，表面疏水性较低。流变学表明，与天然蛋白质相比，水解豌豆蛋白（PPH）基凝胶的储能模量（G'）略有降低。5-15 mM CaCl 增加了 PP 和 PPH 基凝胶的 G'，并降低了蠕变恢复试验中的应变。扫描电子显微镜（SEM）显示，与 PP 凝胶相比，PPH 基凝胶中存在较小的蛋白质聚集体，并且在存在 15 和 25 mM CaCl 时，凝胶网络变得更加致密、更紧凑和更不均匀。凝胶解离测定表明，疏水相互作用和氢键是维持凝胶结构的主要作用力。体外消化表明，与 PP 相比，PPH 基凝胶中的可溶性蛋白质含量高 10%∼30%。CaCl 加量具有浓度依赖性，降低了蛋白质的消化率。结果表明，有限水解和 CaCl 对商业豌豆蛋白的凝胶能力和消化率有相反的影响。这些发现为通过配方和酶预处理开发具有平衡质地和蛋白质营养的豌豆蛋白基食品产品提供了实用的指导原则。
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