Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 110, Issue -, Pages 32-38Publisher
ELSEVIER
DOI: 10.1016/j.molcatb.2014.09.010
Keywords
Lipase; Immobilization; Metal ceramic; Activation; Cinnamyl acetate
Funding
- National Natural Science Foundation of China [51173128, 31071509, 20976125, 21206113]
- 863 Program of China [2012AA06A303, 2013AA102204]
- Ministry of Science and Technology of China [2012YQ090194]
- Beiyang Young Scholar of Tianjin University
- Program of Introducing Talents of Discipline to Universities of China [B06006]
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The metal ceramic powder (MCP) was used for lipase immobilization. The MCP containing Ni2-1 (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 degrees C/min, lipase concentration: 9 mg/mL, immobilization time: 8 h), Ni-MCPlipase 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 degrees 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 degrees C; acetic acid/cinnamyl alcohol: 2:1 in 15.0 mL reaction system), the cinnamyl acetate yield would reach 62.56%. (C) 2014 Elsevier B.V. All rights reserved.
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