We extracted collagen (CL) from the scales of Ctenopharyngodon idella and fabricated a CL self-assembly film. Catalase (CAT) was immobilized on the films using cross-linking, adsorption, and embedding methods. The activity and operational stability of immobilized CAT were investigated, along with the influence of the concentration of glutaraldehyde (GTA) and of the initial concentration of embedded CAT. The results showed that the CL triple helix remained intact. Differential scanning calorimetry data showed that the thermal stability of CL was significantly improved by neutral salt-induced self-aggregation and GTA cross-linking. The immobilized enzyme had high activity and good operational stability. When the enzyme concentration reached 0.5 mg/mL, immobilized enzyme activity of grass carp scales reached a maximum of 2596 U/g, and after twenty-two uses, enzyme activity remained above 50%, and it could be reused >45 times (CAT = 0.5 mg/mL, GTA = 5%, Temperature = 30 °C, pH = 7). Moreover, the optimum temperature and pH of immobilized CAT were 35 °C and 7, respectively, while the same for free CAT was 30 °C and 7, respectively. This indicated that immobilization of CAT has a protective effect.
Keywords: Catalase; Collagen; Enzyme activity; Self-aggregation.
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