Kesan Transglutaminase kepada Ciri Fizikokimia dan Aktiviti Biologi Hidrolisat Sarang Burung Walit

Previous study has shown that edible bird's nest (EBN) glycoprotein can be hydrolysed and recovered as edible bird's nest hydrolysate (EBNh) in the form of powder. This research is a continuous work from previous study, in which different concentrations of transglutaminase enzyme (TG) was applied in reconstituting the shape of EBNh powder using mould, and its effect on the physicochemical properties and bioactivities of EBNh. Enzymatic hydrolysis process showed that EBNh samples had recovery yield exceeding 60% and demonstrated brighter colour than raw EBN. Solubility of EBNh with TG was lower but it can be reconstituted into desirable shape. Spectrum pattern of FTIR for EBNh sample also showed that high authenticity of EBN glycopeptide was obtained. For antioxidant activities, EBNh co -product (EBNh(cp)) exhibited higher DPPH free radical scavenging activity. In short, addition of TG to EBNh has enhanced the physicochemical properties and bioactivities. The finding generates insight on the application and development of EBN products using EBNh with TG with high bioactivities.