Characterization and catalytic properties of a new crude lipase from C. rugosa

Using fed-batch controlled fermenter conditions and oleic acid as the only carbon source, a new crude lipase from Candida rugosa ATCC 14830 (UAB) was produced. This lipase is a mixture of Lip2 (43%) and Lip3 (57%) and shows different composition in isoenzymes than commercial lipase from Sigma, CRL (17% Lip3 and 83% Lip1) and different content in carbohydrates. Both biocatalysts show different catalytic activity in the hydrolysis of triglycerides and in organic synthesis in slightly hydrated organic solvents with aw control: (i) heptyl oleate synthesis, (ii) 2-arylpropionic acids esterification and (iii) acylation of different terpenic alcohols. From the structure–activity scope we show that Lip2 is an isoenzyme, which accepts large molecules – acyl donor or acyl acceptor – and that Lip1 is very active versus unbranched structures but requires water in the microenvironment to be active.