Properties and Stability of Protein-based Films from Red Tilapia (Oreochromis niloticus) Protein Isolate Incorporated with Antioxidant during Storage

Film from fish protein isolate (FPI) from red tilapia (Oreochromis niloticus) muscle prepared at pH 3 and incorporated with 100 ppm Trolox (FPIT film) was prepared and characterized in comparison with film prepared from unwashed mince film (UWM film) during storage of 40 days at room temperature (28-32A degrees C). FPIT film had higher tensile strength (TS) and elongation at break (EAB) but lower water vapor permeability (WVP) than UWM film (p < 0.05). During the storage, FPIT film had much lower thiobarbituric acid reactive substances value than UWM film. Furthermore, FPIT was more transparent and had no yellow discoloration, as evidenced by no change in b* and Delta E* values during the storage of 40 days. Both UWM and FPIT films were stabilized mainly by hydrogen bond, followed by hydrophobic interaction, disulfide bond, and nondisulfide covalent bond. Fourier transforms infrared spectra indicated that FPIT film contained the lower amount of lipids with the lower amplitude of amide B band, compared with UWM film. Higher degradation temperature (Td) was observed in FPIT film, indicating a greater protein-protein interaction in film matrix. FPIT film had smoother surface and cross-section than UWM film. After 40 days of storage, both films had the increase in TS and Td but lower EAB, WVP, and protein solubility. This was more pronounced in UWM film and was associated with the formation of nondisulfide covalent bond in the film network, most likely mediated by the interaction between protein and lipid oxidation products via Maillard reaction. Thus, film from FPI incorporated with antioxidant had the improved mechanical and physical properties without yellow discoloration.