Effects of protein concentration, ionic strength, and heat treatment on the interfacial and emulsifying properties of coconut (Cocos nucifera L.) globulins.

This research aimed to investigate the effects of protein concentration (0.2 %-1.0 %), ionic strength (100-500 mM NaCl), and heat treatment (temperature: 80 and 90℃; time: 15 and 30 min) on the interfacial and emulsifying properties of coconut globulins (CG). When protein concentration was set at 0.2-0.6 %, the interfacial adsorption increased with the increasing of protein concentration. However, the lowest interfacial viscoelasticity was found when CG concentration was 0.6 %. When the protein concentration was higher than 0.6 %, the dilatational viscoelasticity increased with the increasing of protein concentration. The protein concentration showed positive effect on the emulsion stability of CG. The ionic strength showed positive effect on the interfacial adsorption but negative effects on the interfacial viscoelasticity and emulsion stability. Higher temperature and longer heating time brought worse interface behavior. The heated CG (90℃, 30 min) had the worst interfacial behavior but the best emulsion stability.