Abstract
Lipase from Candida rugosa (CrL) was immobilised on highly hydrophobic, octadecyl methacrylate resin (Lifetech™ ECR8806M) via interfacial adsorption. The aim was to produce a stable biocatalyst suitable for use in a range of lipid-modifying reactions. Immobilisation was carried out in 10 mM phosphate buffer (pH 6.0) over 24 h at 21 °C. High protein binding of 58.7 ± 4.9 mg/g dry support accounted for ∼53 % of the applied protein. The activity recovery against tributyrin was 74.0 ± 1.1 %. The specific activity of immobilised CrL against tributyrin was considerably higher than that of Novozym® 435, at 1.79 ± 0.05 and 1.08 ± 0.04 U/mg bound protein, respectively. Incubation with high concentrations (10 % w/v) of both Triton X-100 and SDS resulted in only a small reduction in immobilised lipase activity. Solvent-free synthesis of glycerides by the FFA-saturated immobilised CrL was successful over 6 reaction cycles, with no apparent loss of activity.