Production of an acidic and thermostable lipase of the mesophilic fungus Penicillium simplicissimum by solid-state fermentation.
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.
Gutarra
Melissa L E
ML
Universidade Federal do Rio de Janeiro, IQ, Departamento de Bioquímica, Brazil.
Godoy
Mateus G
MG
Maugeri
Francisco
F
Rodrigues
Maria Isabel
MI
Freire
Denise M G
DM
Castilho
Leda R
LR
D000143:Acids / Q000378:metabolism*; D000704:Analysis of Variance; D001426:Bacterial Proteins; D005285:Fermentation; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000096:biosynthesis*; D010407:Penicillium / Q000201:enzymology* / Q000254:growth & development; D012015:Reference Standards; D012044:Regression Analysis; D013379:Substrate Specificity; D013499:Surface Properties; D013696:Temperature; D013997:Time Factors
D000143:Acids; D001426:Bacterial Proteins; D008049:Lipase; C428386:thermostable lipase