Gelation is an important techno-functionality for novel protein sources. Yet, only one study has focused on the gelling potential of concentrates from the microalgae Spirulina, despite its potential as a sustainable protein source. That study reported relatively low stiffness, hindering the application. The current study focuses on Spirulina protein concentrate (SPC) gel characterization and the utilization of high-pressure homogenization (HPH) before thermal gelation to improve gel properties. We reveal that the gelation is possible at pH 6.5, yet not at more acidic pH due to insufficient protein solubility. Phycobiliproteins - the main proteins in SPC, aren't responsible for gel network formation. The application of HPH at 50 MPa, as a pretreatment increased protein solubility by 91%. The surface hydrophobicity increased by at least 212% while decreasing particle size. Those HPH effects on SPC dispersion were correlated with an increase in gel stiffness and a decrease in the gelation point.

凝胶化是新型蛋白质来源的重要技术功能。然而，尽管螺旋藻具有作为可持续蛋白质来源的潜力，但只有一项研究关注了来自微藻螺旋藻的浓缩物的胶凝潜力。该研究报告了相对较低的刚度，阻碍了应用。目前的研究重点是螺旋藻蛋白质浓缩物 (SPC) 凝胶表征和在热凝胶化之前利用高压均质化 (HPH) 来改善凝胶特性。我们发现凝胶在 pH 6.5 下是可能的，但由于蛋白质溶解度不足，在更酸性的 pH 下则不能。藻胆蛋白 - SPC 中的主要蛋白质，不负责凝胶网络的形成。应用 50 MPa 的 HPH 作为预处理将蛋白质溶解度提高了 91%。表面疏水性增加了至少 212%，同时减小了粒径。这些 HPH 对 SPC 分散的影响与凝胶刚度的增加和凝胶点的降低相关。