Immobilization of Candida antarctica lipase B by covalent attachment to green coconut fiber.
The objective of this study was to covalently immobilize Candida antarctica type B lipase (CALB) onto silanized green coconut fibers. Variables known to control the number of bonds between enzyme and support were evaluated including contact time, pH, and final reduction with sodium borohydride. Optimal conditions for lipase immobilization were found to be 2 h incubation at both pH 7.0 and 10.0. Thermal stability studies at 60 degrees C showed that the immobilized lipase prepared at pH 10.0 (CALB-10) was 363-fold more stable than the soluble enzyme and 5.4-fold more stable than the biocatalyst prepared at pH 7.0 (CALB-7). CALB-7 was found to have higher specific activity and better stability when stored at 5 degrees C. When sodium borohydride was used as reducing agent on CALB-10 there were no improvement in storage stability and at 60 degrees C stability was reduced for both CALB-7 and CALB-10.
Brígida
Ana I S
AI
Departamento De Engenharia Química, Campus Do Pici, Bloco 709, Universidade Federal Do Ceará, 60455-760, Fortaleza, CE, Brazil.
Pinheiro
Alvaro D T
AD
Ferreira
Andrea L O
AL
Pinto
Gustavo A S
GA
Gonçalves
Luciana R B
LR
D003059:Cocos / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D005656:Fungal Proteins; D008049:Lipase / Q000737:chemistry*
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D008049:Lipase; C431349:lipase B, Candida antarctica