Intensification of lipase performance for long-term operation by immobilization on controlled pore silica in presence of polyethylene glycol.
In agreement with previous studies, promising results were obtained when lipase was immobilized on controlled pore silica (CPS) in the presence of polyethylene glycol (PEG 1500). This methodology rendered immobilized derivatives with higher operational stability than those lacking PEG 1500. This article extends the scope of this approach by evaluating the combined effects of PEG concentration and lipase loading employing a multivariate statistical approach. A 2(2) factorial design with center point was adopted for a full understanding of these effects and their interactions. Conditions that maximize the immobilization yield were different from those attained for the biocatalyst's operational stability. Possible reasons for the increase in both activity and stability of lipase immobilized on CPS in the presence of PEG 1500 are discussed in light of the influence of surface hydrophilic/hydrophobic balance.
Soares
Cleide M F
CM
Department of Chemical Engineering, Faculdade de Engenharia Química de Lorena, SP, Brazil.
De Castro
Heizir F
HF
Santana
M Helena A
MH
Zanin
Gisella M
GM
D002175:Candida / Q000201:enzymology; D002384:Catalysis; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology*; D012822:Silicon Dioxide
D004800:Enzymes, Immobilized; D011092:Polyethylene Glycols; D012822:Silicon Dioxide; D008049:Lipase