LAUSR

Herein, we report the preparation of a cross-linked protein-metal hybrid nanoflower (NF) system for laccase immobilization. The immobilized laccase showed effective encapsulation yield and activity recovery of 78.1% and 204%, respectively. The catalytic efficiency (kcatVmax-1) of cross-linked NF (CL-NF) was 2.2-fold more than that of free laccase. The CL-NF also exhibited significantly higher stability towards pH and temperature changes. It exhibited excellent storage stability and tolerance towards solvents and inhibitors as compared with the free enzyme. After 10 cycles of reuses, the NF and CL-NF laccase showed 41.2% and 92.3% residual activity, respectively. The CL-NF showed high oxidation potential, 265% that of the free enzyme, towards phenolic compounds. The CL-NF laccase retained the residual decolorization efficiency of up to 84.6% for synthetic dyes under repeated batch conditions of 10 cycles. These results suggested that the preparation of CL-NF is an effective approach to enhance the enzymatic properties and has great potential in many industrial applications.