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

Abstract 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%.