Abstract：
Microalgae protein holds great potential for various applications in the food industry. However, the current knowledge regarding microalgae protein remains limited, with little information available on its functional properties. Furthermore, the relationship between its molecular structure and functional properties is not well defined, which limits its application in food processing. This study aims to addresses these gaps though an analysis of the emulsibility and foamability of various soluble protein isolates from two species of Spirulina (Arthospira platensis and Spirulina platensis), and the functional properties of Spirulina protein isolates in relation to its molecular structure and charge state. Results revealed that the degree of cross-linking and aggregation or folding and curling of protein tertiary structures was higher in the highly soluble Spirulina protein isolates (AP50% and SP50%) than in the low-solubility isolates (AP30% and SP30%). The foaming capacity (FC) of AP50% and SP50% was found to be lower than that of AP30% and SP30%. Spirulina protein isolates can stably adsorb at the air-water interface for at least 20 min and possessed good interfacial activity. A high pH value was found to promote cross-linking of protein particles at the oil-water interface, thereby reinforcing the internal network structure of emulsions and increasing viscosity. These findings provide preliminary insights for potential applications of Spirulina protein isolates in food production, especially towards quality improvement.
摘要：
微藻蛋白在食品工业中的各种应用中具有巨大的潜力。然而,目前关于微藻蛋白的知识仍然有限，关于其功能特性的信息很少。此外，其分子结构和功能性质之间的关系还没有很好的定义，限制了其在食品加工中的应用。本研究旨在通过分析来自两种螺旋藻（螺旋藻和螺旋藻）的各种可溶性蛋白分离物的乳化性和起泡性，来解决这些差距。以及螺旋藻分离蛋白的功能特性与其分子结构和电荷状态有关。结果表明，高可溶性螺旋藻蛋白分离物（AP50％和SP50％）的蛋白质三级结构的交联和聚集或折叠和卷曲程度高于低溶解度分离物（AP30％和SP30％）。发现AP50%和SP50%的发泡能力(FC)低于AP30%和SP30%的发泡能力。螺旋藻蛋白分离物可以在空气-水界面稳定吸附至少20分钟，并具有良好的界面活性。发现高pH值会促进蛋白质颗粒在油-水界面的交联，从而增强乳液的内部网络结构并增加粘度。这些发现为螺旋藻蛋白分离物在食品生产中的潜在应用提供了初步见解。特别是质量改进。
