Zinc sulfide-chitosan hybrid nanoparticles as a robust surface for immobilization of Sillago sihama α-amylase.

In the present study, zinc sulfide-chitosan hybrid nanoparticles synthesized by chemical deposition were used as a matrix for the immobilization of purified α-amylase extracted from Sillago sihama (Forsskal, 1775). In this regard, the size and morphological structure of zinc sulfide-chitosan hybrid nanoparticles before and after the stabilization process were evaluated using FT-IR, DLS methods, as well as SEM and TEM electron microscopy, and EDS analyses. Then, the efficiency of the immobilized enzyme was measured in terms of temperature, optimal pH, stability at the critical temperature, and pH values. Immobilization of α-amylase on zinc sulfide -chitosan hybrid nanoparticles increased the long-term stability, as well as its endurance to critical temperatures and pH values; however, the optimal temperature and pH values of the enzyme were not altered following the immobilization process. The kinetic parameters of the enzyme were also changed during immobilization. Enzyme immobilization increased the K, whereas decreased the catalytic efficiency (K / K) of the immobilized enzyme compared with the free enzyme. These results are very important as, in most cases, enzyme immobilization reduces the activity and catalytic efficiency of enzymes. The nano-enzyme produced in this study, due to its high temperature, and pH stability, could be a good candidate for industrial applications, especially in the food industry.