Production of Extracellular Lipases by<i>Penicillium cyclopium</i>Purification and Characterization of a Partial Acylglycerol Lipase

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  • CHAHINIAN Henri
    Laboratory of Applied Biological Chemistry, Faculty of Sciences and Technology
  • VANOT Guillaume
    Laboratory of Applied Biological Chemistry, Faculty of Sciences and Technology
  • IBRIK Aida
    Laboratory of Applied Biological Chemistry, Faculty of Sciences and Technology
  • RUGANI Nathalie
    Laboratory of Microbiology, Faculty of Sciences and Technology
  • SARDA Louis
    Laboratory of Biochemistry, Faculty of Sciences, St-Charles, University of Provence
  • COMEAU Louis-Claude
    Laboratory of Applied Biological Chemistry, Faculty of Sciences and Technology

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  • Production of Extracellular Lipases by Penicillium cyclopium Purification and Characterization of a Partial Acylglycerol Lipase.

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  Penicillium cyclopium, grown in stationary culture, produces a type I lipase specific for triacylglycerols while, in shaken culture, it produces a type II lipase only active on partial acylglycerols. Lipase II has been purified 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 deglycosylation. Activity of lipase II is maximal at pH 7.0 and 40°C. The enzyme is stable from pH 4.5 to 7.0. Activity is rapidly lost at temperatures above 50°C. The enzyme specifically hydrolyzes monoacylglycerols and diacylglycerols, especially of medium chain fatty acids. The sequence 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 lanuginosa and Aspergillus oryzae, but is different from Penicillium cyclopium 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 Penicillium expansum lipase, of which 16 out of the 20 first amino acid residues are similar to Penicillium cyclopium lipase I.<br>

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