Lipase A and B from Geotrichum candidum CMICC 335426 were functionally expressed and secreted in Pichia pastoris. Lipase B exhibits a unique substrate specificity for long-chain cis-Δ9 unsaturated triacylglycerols. Thus, using different cultivation conditions, the production of recombinant lipase B was optimised, yielding 200 000 Units per liter culture. After overexpression lipase B was purified by diafiltration (372 U/mg). The investigated enzyme properties were comparable to those reported for the native enzyme.
Bibliographical noteFunding Information:
We would like to thank Eckart Bonacker for performing the cultivations and for his technical assistance. We thank Dr. Chris Davies (Unilever, Colworth House) for providing us the lipases genes. Elisabetta Catoni gratefully acknowledges a scholarship from the European Commision as part of an European Community Training Project (BIO4-CT96–5059, ΔG12-SSMA).