Abstract
Crosslinking is essential for maintaining the integrity of protein-based nanoparticles against environmental fluctuations. However, conventional crosslinkers (e.g. glutaraldehyde) are usually toxic and environmental unfriendly. In this study, a tyrosinase-aided crosslinking procedure was developed and compared to the conventional glutaraldehyde-based process. Sodium caseinate (SC) nanoparticles were synthesized by ionic gelation or desolvation under aqueous or alcoholic condition, respectively. The nanoparticles were stabilized by different crosslinkers and challenged under simulated environmental stress, including acidification and antisolvent removal. A simple procedure based on dynamic light scattering (DLS) was developed to evaluate the particle integrity, using the retention of particle size and count rate as indicators. Satisfying crosslinking was observed for the ionic gelation procedure in the presence of tyrosinase (10 U/mol SC) combined with two phenols (catechol or chlorogenic acid, 2.5 mol/mol SC). In comparison, a higher dose of glutaraldehyde (7.5 mol/mol SC) was required for achieving a comparable crosslinking effect. For the desolvation procedure, the efficacies for both glutaraldehyde and tyrosinase-phenol blends decreased, although they were still significant, and glutaraldehyde exhibited better crosslinking effect. The results from the DLS study were in consistence with those obtained from scanning electron microscopy. Overall, tyrosinase-aided oxidation is a competitive, low-toxicity approach for crosslinking protein-based nanostructures.
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