Production of extracellular lipases by Penicillium cyclopium purification and characterization of a partial acylglycerol lipase

Penicillium cyclopium, grown in stationary culture, produces a type I lipas e specific for triacylglycerols while, in shaken culture, it produces a typ e II lipase only active on partial acylglycerols. Lipase II has been purifi ed by ammonium sulfate precipitation and chromatographies on Sephadex G-75 and DEAE-Sephadex. The enzyme exists in several glycosylated forms of 40-43 kDa, which can be converted to a single protein of 37 kDa by enzymatic deg lycosylation. Activity of lipase II is maximal at pH 7.0 and 40 degrees C. The enzyme is stable from pH 4.5 to 7.0. Activity is rapidly lost at temper atures above 50 degrees C. The enzyme specifically hydrolyzes monoacylglyce rols and diacylglycerols, especially of medium chain fatty acids. The seque nce of the 20 First amino acid residues is similar to the N-terminal region of P. camembertii lipase and partially similar to lipases from Humicola la nuginosa and Aspergillus oryzae, but is different from Penicillium cyclopiu m lipase I. However, it can be observed that residues of valine and serine at positions 2 and 5 in Penicillium cyclopium lipase II are conserved in Pe nicillium expansum lipase, of which 16 out of the 20 first amino acid resid ues are similar to Penicillium cyclopium lipase I.