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.