Second- and third-generation biodiesel production with immobilised recombinant Rhizopus oryzae lipase: Influence of the support, substrate acidity and bioprocess scale-up

Rhizopus oryzae lipase immobilised onto differently functionalised polymethacrylate (Purolite (R)) and magnetite superparamagnetic supports was assessed as a catalyst for biodiesel production with pomace oil. The presence of surface hydrocarbon chains increased the operational stability of the biocatalysts supported on Purolite (R) and superparamagnetic particles up to 9 and 2 times, respectively. By contrast, the presence of functional groups had no effect on the initial transesterification rate, which was twice higher with the lipase immobilised onto Purolite (R). Also, functionalising Purolite (R) with epoxide and octadecyl groups led to the highest biodiesel and volumetric productivity. This biocatalyst with other substrates including makauba, jatropha, waste cooking oil, and microbial oil, led to similar initial reaction rates. However, simply raising substrate acidity from 0.5 to 2% increased the operational stability of the biocatalysts 15 times. A synergistic effect between acyl-acceptor concentration and substrate acidity was observed. The transesterification reaction was successfully scaled up to 50 mL.

Automated summary

Immobilizing Rhizopus oryzae lipase on Purolite (R) and magnetite superparamagnetic supports increased operational stability; functionalizing Purolite (R) enhanced biodiesel and volumetric productivity; raising substrate acidity significantly improved operational stability of the biocatalyst.