<p>This study explores the impact of Moringa oleifera seed protein (MOSSP) and chitosan (CS) on emulsion stability, focusing on molecular weight and protein concentration. The results revealed that CS’s molecular weight significantly influences the emulsifying activity and MOSSP binding capacity. Notably, the presence of high molecular weight CS resulted in a decrease in MOSSP’s emulsifying activity. Emulsions stabilized by MOSSP-CS30 exhibit superior stability, attributed to the strong binding interactions between MOSSP and high molecular weight CS. This interaction induced partial protein conformational changes and zeta potential (ζ potential) alterations. The MOSSP concentration also played a pivotal role in emulsion characteristics, with decreased emulsifying activity index (EAI) and emulsion stability index (ESI), leading to larger droplet sizes despite increased turbidity. Emulsions containing 0.5% and 1% MOSSP-CS30 displayed higher turbidity values of 0.637 and 0.665, respectively, with the 1% MOSSP-CS30 emulsion showcasing the smallest droplet size. The thermal stability of the 0.5% MOSSP-CS30 emulsion was optimal at 83.6%. These findings suggested that the bridging monolayer of MOSSP-CS emulsions was crucial for stability maintenance and would benefit food product formulation, particularly in industries requiring stable emulsions and could serve as a vehicle for encapsulating and protecting sensitive bioactive compounds, enhancing their bioavailability and efficacy.</p>