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Hindi Synthesis of ethyl acetate from purified lipase of Aspergillus fumigatus
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Copyright: © 2020 . This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
Lipases are ubiquitous biological macromolecules which have many industrial and environmental applications. Lipase was purified from Aspergillus fumigatus by using Octyl Sepharose column chromatography. The enzyme was purified by ammonium sulfate precipitation and hydrophobic interaction chromatography which resulted in 7-fold purification. The molecular weight of protein using Native-PAGE was found to be 70 kDa. The apparent molecular weight by SDS-PAGE was found to be 35 kDa which indicated that the enzyme was homodimer. The optimum temperature and pH for activity of the enzyme was found to be 40°C and 9.0 respectively. The kinetic parameters Vmax and Km of the purified lipase were 10.42 μmol min−1 mg−1and 9.89 mM respectively. Ethyl acetate was synthesized using purified lipase from ethanol and acetic acid and was analyzed by GC/MS. The sample fragment ion at 41 and 63 m/z indicated the presence of ethyl acetate in the sample.
