Immobilization of Candida antarctica lipase B by adsorption in organic medium.
Candida antarctica lipase B (CALB) was immobilized on the macroporous resin by physical adsorption in organic medium. The immobilization was performed in 5 mL isooctane, and the immobilization conditions were optimized. The results were achieved with the mass ratio of lipase to support 1:80, the buffer of pH 6.0, initial addition of PBS 75 microL, and immobilization time of two hours at 30 degrees C. Under the optimal conditions, the activity recovery was 83.3%. IM-CALB presented enhanced pH and thermal stability compared to the free lipase, and showed comparable stability with the commercial Novozym 435, after 7 times repeated use for catalyzing the synthesis of ethyl lactate, 56.9% of its initial activity was retained, and only 24.7% was retained when used for catalyzing the hydrolysis of olive oil.
Sun
Jiangna
J
Department of Bioengineering, School of Chemical Engineering, Hebei University of Technology, Tianjin 300130, China.
Jiang
Yanjun
Y
Zhou
Liya
L
Gao
Jing
J
D000327:Adsorption; D055162:Biocatalysis; D002021:Buffers; D003470:Culture Media / Q000737:chemistry*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D012997:Solvents / Q000737:chemistry; D013696:Temperature
D002021:Buffers; D003470:Culture Media; D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D012997:Solvents; C093667:Novozyme 435; D008049:Lipase; C431349:lipase B, Candida antarctica