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®) 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® 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®.