To improve functional properties of food proteins, homologous or heterologous ${eta}-casein$ and 11S globulin(glycinin) from animal and vegetable proteins, respectively, were bio-hybridized using transglutaminase(MTGase). Susceptibility was confirmed by SDS-PAGE, particle size analyzed, and emulsion stability tested using Reddy and Fogler method, To determine how bio-hybridized protein influences emulsion stability, protein bound on oil droplet was investigated using Scanning Electron Microscopy (SEM). formation of bio-hybridized protein band was detected among homologous and heterologous proteins, with heterologous protein forming weak band in oligomer form. Homologous ${eta}-casein$ protein showed high emulsion stability, while homologous glycinin showed almost no stability. Stability of heterologous ${eta}-casein$ and glycinin protein was higher than that of glycinin. SEM photographs showed even distribution of bio-hybridized proteins on oil droplet improved stability.