FOOD SCIENCE ›› 2011, Vol. 32 ›› Issue (21): 171-176.doi: 10.7506/spkx1002-6630-201121035

• Bioengineering • Previous Articles     Next Articles

Immobilization and Characterization of Lipase Immobilized onto Cellulose Acetate-Polytetrafluoroethylene Composite Membrane

LIANG Dan-qiong1,ZHOU Xiao-dan2,SHI Min2,WANG Xue2,YU Dian-yu2,*   

  1. (1. Heilongjiang Research Institute of Pulp and Paper Industry, Mudanjiang 157013, China; 2. College of Food Science, Northeast Agricultural University, Harbin 150030, China)
  • Online:2011-11-15 Published:2011-11-11

Abstract: In the present work, we immobilized lipase onto cellulose acetate (CA)-polytetrafluoroethylene (PTFE) composite membrane by a combined method of adsorption and cross-linking. The effects of different immobilization conditions such as immobilization temperature, adsorption time, lipase concentration, cross-linking time and cross-linking agent concentration on lipase immobilization efficiency and catalytic activity were explored. Immobilized lipase was also characterized. The optimal immobilization conditions were reaction temperature of 25 ℃, adsorption time of 2 h, lipase concentration of 0.02 g/mL, crosslinking time of 3 h, and cross-linking agent concentration of 0.2%. Under the optimal immobilization conditions, the maximum activity of immobilized lipase reached up to 17.2 U/cm2. The optimal temperature and pH of immobilized lipase were 35 ℃ and 8.5, respectively, which exhibited a decrease by 5 ℃ and shift to alkaline side by 1.0 when compared with the free enzyme. After repeated use for 10 times for 10 h each time, the residual activity was still up to 55.5%. The SEM micrographs revealed better immobilization of the enzyme on CA-PTFE composite membrane.

Key words: CA-PTFE composite membrane, lipase, immobilization, lipase activity

CLC Number: