Immobilisation of Candida rugosa lipase on a highly hydrophobic support: A stable immobilised lipase suitable for non-aqueous synthesis.

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.

SUBMITTER: Kurtovic I 

PROVIDER: S-EPMC7566202 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature