BACKGROUND: The development of biodegradable materials, especially those from renewable sources, is important to reduce the impact of plastic waste on the environment. On the other hand, protein-based lms have high solubility in water, in addition to limited mechanical properties, which makes their application in high humidity environments a challenge. The enzyme transglutaminase (TGase) can reduce the interaction of gelatin lms with water, improving these properties, while improving the mechanical properties.Therefore, this study aimed to determine the best condition for using the TGase enzyme, through variations in the gelatin and enzyme mass, in addition to the time that the enzyme acts on the gelatin, evaluating the properties tensile strength, elongation, and solubility in water. In a second set of experiments gelatin amount was kept xed at 4%, and other proportions of an enzyme (1% and 5% w/w gelatin) were studied, evaluating beyond these properties the degradation in simulated soil through thermogravimetry analysis and Fourrier Transform Infrared Spectrometer (FTIR).RESULTS: It was concluded that the higher concentration of TGase (5%) promoted a greater reduction in the solubility of the lms, making the lms more resistant to biodegradation, facilitating their application due to the increase in their useful life. CONCLUSION: At the end of the degradation test, it was noticed that the lms were degraded, presenting the potential for substitution of polymers of fossil origin, which could be an alternative to the problem of polymeric residues in the environment.
HighlightsThe addition of the enzyme decreased the solubility of the lms;Films with the enzyme have increased resistance to biodegradation when compared to lms without the enzyme.Gelatin lms with and without enzyme have been completely degraded when expose to soil.