Abstract
In this investigation, a nano-support containing cellulose nanocrystals – polydopamine (CP) was functionalized with glutaraldehyde (G) and utilized to immobilize papain. The properties of the supports and stabilized enzyme were characterized by TEM, SEM, DLS, Zeta-potential, FTIR, and EDS analyses. The optimal temperature of both papain forms was 60 °C, while the optimal pH value of the stabilized papain shifted from 7 to 8 after immobilization. The immobilized enzyme preparations showed higher stability at 80 and 90 °C and under acidic and alkaline conditions compared to the free enzyme. CPG-papain stability was higher than that of CP-papain. The Km values for free and immobilized papain on CP and CPG were 3.92, 3, and 2.74 mM respectively. Kcat values were 9.05, 15.18, and 11.59 min−1 and catalytic efficiency values were 2.3, 5.05, and 4.23 mM−1.min−1. Additionally, the potential advantages of using a silver nanohydrid support were assessed. Although silver nanoparticles conveyed some catalytic activity to the final biocatalysts, they also caused a decrease in stability and activity of the immobilized papain. Therefore, the non-hybrid supports CP and CPG were more suitable candidates for the immobilization of papain than the hybrid supports.
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