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Cordyceps militaris , an entomopathogenic Cordyceps mushroom, is a crucial ethnopharmacological agricultural product with applications in traditional oriental remedies in East Asia. Since lipases are reported to serve as key enzymatic equipment for entomopathogenic fungi during the host infection, the presence of various lipases with different biochemical features in C. militaris was elucidated. Three lipases from C. militaris (CML) of 60–70 kDa were isolated according to protein hydrophobicity; isoform relationships were identified by peptide mapping using liquid chromatography–electrospray ionization–tandem mass spectrometry. The CML isoforms exhibited distinct substrate specificities, which were related to the hydrophobicity of each isoform. Furthermore, the integral stereoselectivity of each lipase towards trioleoylglycerol diverged into two classes (sn -1,3 and sn -2 regioselectivity) that are rare in canonical fungal lipases. Overall, our results demonstrate that C. militaris secretes lipase isoforms with cocktail-like enzyme functions that may contribute to the entomopathogenic life cycle of C. militaris. Each CML isoform has distinct advantages for biocatalyst applications in the food and oleochemical industries. [Display omitted] • Three lipase isoforms were isolated from entomopathogenic Cordyceps mushroom, Cordyceps militaris. • The isoforms exhibited divergent substrate specificities correlated to their protein hydrophobicity. • The isoforms displayed integral stereoselectivities in two class; sn-1,3 and sn-2 regioselectivity. • The combination of isoforms may provide cocktail-like enzymatic advantages in entomopathogenic life cycle of C. militaris. [ABSTRACT FROM AUTHOR]