Department of Chemical Engineering, Universidad de La Frontera, Av. Francisco Salazar, 01145, Temuco, Chile; Scientific and Technological Bioresources Nucleus-BIOREN, Universidad de La Frontera, Av. Francisco Salazar, 01145, Temuco, Chile. Electronic address: [Email]
The immobilization of Candida rugosa lipase (CRL) onto biochar was studied in a series of batch experiments. CRL sorption behavior was evaluated as a function of pH, enzyme concentration, temperature and ionic strength. As the immobilized lipase was used for the catalytic esterification of oleic acid, its resistance to solvents and thermal stability were evaluated. CRL adsorption increased by increasing temperature, and with higher pH, reaching a maximum at pH 7.0. Immobilization increased lipase stability at 40 °C by more than 80% when compared to the free enzyme. Moreover, immobilized CRL showed high stability in the presence of tert-butanol, which prevents premature deactivation of the enzyme caused by alcohols during the reaction. Immobilization of CRL increased the oleic acid conversion rate. Our results suggest that biochar is a highly promising material for the immobilization of CRL lipase for the catalytic production of esters.