Catalytic, Kinetic and Thermodynamic Characteristics of an Extracellular Lipase from Penicillium notatum

Saima Rehman, Haq Nawaz Bhatti, Muhammad Bilal, Muhammad Asgher, Ping Wang

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8 Scopus citations


Abstract: Lipase of Penicillium notatum was purified to electrophoretic homogeneity by ammonium sulphate precipitation, ion-exchange, and hydrophobic interaction chromatography. The purified enzyme displayed a solitary band in the 46-kDa region on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS–PAGE). The pH and temperature optima were found to be 9.5 and 40 °C, respectively. It showed stability over broad pH range (pH 6.0–12) and higher thermal tolerance with half-lives (t1/2) of 8.25, 3.2, 1.12, and 0.58 h at 40, 50, 60 and 70 °C, respectively. The Kmand Vmaxvalues for p-nitro phenyl palmitate (pNPP) hydrolysis were 3.33 mM and 232.6 µmol/mL min−1, respectively. The energy of activation for denaturation Ea(d)was 81.1 kJ/mol, whereas the entropy (ΔS*), enthalpy (ΔH*) and free energy (ΔG*) of thermal inactivation of lipase were recorded to be −0.083 Jmol−lK−l, 78.48 and 104.54 kJ/mol, respectively, at 40 °C. The enzymatic activity was substantially improved by Ca2+and Mg2+, and suppressed in the presence of Co2+,Cd2+, Pb2+and Fe3+ions to various levels. Exposure to hydrophobic environment did not affect the enzyme stability; however, protease solution deactivated the enzyme. Considering all these properties, this fungal lipase would be an interesting candidate for future organic synthesis application. Graphical Abstract: [Figure not available: see fulltext.]

Original languageEnglish (US)
Pages (from-to)281-291
Number of pages11
JournalCatalysis Letters
Issue number1
StatePublished - Jan 2017


  • Kinetics
  • Lipase
  • Penicillium notatum
  • Purification
  • Thermodynamics

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