Lipase immobilized on novel ceramic supporter with Ni activation for efficient cinnamyl acetate synthesis

The metal ceramic powder (MCP) was used for lipase immobilization. The MCP containing Ni 2+ (Ni-MCP) exhibited the best affinity to lipase . The effects of heating rate, lipase concentration and immobilization time on immobilized lipase (Ni-MCP-lipase) activity were measured. Under the optimal preparation conditions (heating rate: 1   °C/min, lipase concentration: 9   mg/mL, immobilization time: 8   h), Ni-MCP-lipase could obtain 1.4   U/g and 216% of activity yield. The Ni-MCP-lipase, with improved thermal stability and storage stability, had optimal pH value of 6.0 and optimal temperature of 40   °C. The characterizations clarified the effect of heating rate on Ni-MCP-lipase activity, and confirmed that lipase had been efficiently immobilized on Ni-MCP surface. Finally, cinnamyl acetate synthesis demonstrated that Ni-MCP-lipase had improved efficiency compared with free lipase. Under the optimal reaction conditions (Ni-MCP-lipase loading: 3   g; reaction temperature: 35   °C; acetic acid/cinnamyl alcohol: 2:1 in 15.0   mL reaction system), the cinnamyl acetate yield would reach 62.56%.