Expression, purification, refolding, and enzymatic characterization of two secretory phospholipases A 2 from Neurospora crassa

•Two secretory phospholipases A2 from the filamentous fungus Neurospora crassa were expressed as inclusion bodies in E. coli.•High hydrostatic pressure method was used to refold both proteins.•Both proteins displayed Ca2+-dependent lypolytic activity.•Mass spectrometry analysis demonstrated that both proteins preferentially hydrolyzed the sn-2 ester linkage of phosphatidylcholine and phosphatidylethanolamine.