English 
Spanish 
Chinese 
Russian 
German 
French 
Portuguese 
Hindi 当社グループは 3,000 以上の世界的なカンファレンスシリーズ 米国、ヨーロッパ、世界中で毎年イベントが開催されます。 1,000 のより科学的な学会からの支援を受けたアジア および 700 以上の オープン アクセスを発行ジャーナルには 50,000 人以上の著名人が掲載されており、科学者が編集委員として名高い
。オープンアクセスジャーナルはより多くの読者と引用を獲得
700 ジャーナル と 15,000,000 人の読者 各ジャーナルは 25,000 人以上の読者を獲得
抽象的な
Synthesis of ethyl acetate from purified lipase of Aspergillus fumigatus
Reena Gupta
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.