Production of an acidic and thermostable lipase of the mesophilic fungus Penicillium simplicissimum by solid-state fermentation

Bioresour Technol. 2009 Nov;100(21):5249-54. doi: 10.1016/j.biortech.2008.08.050. Epub 2009 Jun 26.

Abstract

The production of a lipase by a wild-type Brazilian strain of Penicillium simplicissimum in solid-state fermentation of babassu cake, an abundant residue of the oil industry, was studied. The enzyme production reached about 90 U/g in 72 h, with a specific activity of 4.5 U/mg of total proteins. The crude lipase showed high activities at 35-60 degrees C and pH 4.0-6.0, with a maximum activity at 50 degrees C and pH 4.0-5.0. Enzyme stability was enhanced at pH 5.0 and 6.0, with a maximum half-life of 5.02 h at 50 degrees C and pH 5.0. Thus, this lipase shows a thermophilic and thermostable behavior, what is not common among lipases from mesophilic filamentous fungi. The crude enzyme catalysed the hydrolysis of triglycerides and p-nitrophenyl esters (C4:0-C18:0), preferably acting on substrates with medium-chain fatty acids. This non-purified lipase in addition to interesting properties showed a reduced production cost making feasible its applicability in many fields.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acids / metabolism*
  • Analysis of Variance
  • Bacterial Proteins
  • Fermentation*
  • Hydrogen-Ion Concentration
  • Lipase / biosynthesis*
  • Penicillium / enzymology*
  • Penicillium / growth & development
  • Reference Standards
  • Regression Analysis
  • Substrate Specificity
  • Surface Properties
  • Temperature
  • Time Factors

Substances

  • Acids
  • Bacterial Proteins
  • Lipase
  • thermostable lipase