Effects of molecular structure and charge state on the foaming and emulsifying properties of Spirulina protein isolates

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.