TY - JOUR
T1 - Catalytic, Kinetic and Thermodynamic Characteristics of an Extracellular Lipase from Penicillium notatum
AU - Rehman, Saima
AU - Bhatti, Haq Nawaz
AU - Bilal, Muhammad
AU - Asgher, Muhammad
AU - Wang, Ping
N1 - Publisher Copyright:
© 2016, Springer Science+Business Media New York.
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2017/1
Y1 - 2017/1
N2 - 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.]
AB - 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.]
KW - Kinetics
KW - Lipase
KW - Penicillium notatum
KW - Purification
KW - Thermodynamics
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U2 - 10.1007/s10562-016-1931-2
DO - 10.1007/s10562-016-1931-2
M3 - Article
AN - SCOPUS:84997403817
VL - 147
SP - 281
EP - 291
JO - Catalysis Letters
JF - Catalysis Letters
SN - 1011-372X
IS - 1
ER -