Two lipases from Candida antarctica: cloning and expression in Aspergillus oryzae

The basidiomycetous yeast Candida antarctica expresses two lipases that possess widely different properties. The genes LIPA and LIPB encoding both lipases were cloned and sequenced. Both lipases were secreted efficiently from Aspergillus oryzae transformed with lipase expression plasmids. N-Glycosylation was slightly more extensive in the heterologously expressed enzymes than in those purified from C. antarctica, but the enzymatic characteristics were retained. Both enzymes are encoded as preproenzymes. Proteolytic processing of the primary translation product was efficient in A. oryzae and resulted in the same N-terminals as in C. antarctica. Modifications or deletions of the propeptide of lipase component B did not prevent efficient secretion of active lipase from A. oryzae. Alternative proteolytic processing of the modified propeptides was detected.