Optimization of culture conditions and properties of lipase from Penicillium camembertii Thom PG-3 |
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| Institution: | 1. Department of Biochemical Engineering, Beijing University of Chemical Technology, Beijing 100029, PR China;2. Institute of Microbiology, Academic Sinica, Beijing 100080, PR China;1. Department of Physical Medicine and Rehabilitation, Cleveland, OH, USA;2. Department of Medicine, Cleveland, OH, USA;3. Department of Research, Case Western Reserve University, MetroHealth Medical Center, 2500 MetroHealth Drive, Cleveland, OH, USA;4. Research Service, Louis Stokes Cleveland VA Medical Center, 10701, East Boulevard, Cleveland, OH, USA;1. Institute of Reproductive and Child Health/Ministry of Health Key Laboratory of Reproductive Health, Peking University Health Science Center, Beijing 100191, China;2. Department of Epidemiology and Health Statistics, School of Public Health, Peking University Health Science Center, Beijing 100191, China;3. Departments of Pediatrics, Environmental Medicine and Population Health, New York University School of Medicine, New York 10016, USA;4. NYU Wagner School of Public Service, New York 10012, USA;5. NYU Steinhardt School of Culture, Education and Human Development, New York 10003, USA;1. Department of Chemistry of Natural and Microbial Products, National Research Centre, Dokki, Cairo, 12622, Egypt;2. Department of Genetics and Cytology, National Research Centre, Dokki, Cairo, 12622, Egypt;3. Department of Microbiology, Faculty of Science, Ain Shams University, Abbassia, Cairo, 11566, Egypt;1. Key Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People’s Republic of China;2. National Key Laboratory of Agro-Microbiology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People’s Republic of China;3. College of Food Science and Technology, Huazhong Agricultural University, Wuhan, 430070, People’s Republic of China |
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| Abstract: | The culture medium including nitrogen source, carbon source and metal ions, for lipase from Penicillium camembertii Thom PG-3 was optimized and the optimal medium consisted of soybean meal (fat free) 4%, Jojoba oil 0.5%, (NH4)2HPO4, 0.1% Tween 60, initial pH 6.4 and the inoculation was at 28 °C for 96 h. The lipase activity produced was enhanced 3.9-fold and reached 500 U/ml. The lipase was purified 19.8-fold by pH precipitation, ethanol precipitation and ammonium sulphate precipitation as well as DEAE-cellulose chromatography. The purified lipase showed one polypeptide band in SDS-polyacrylamide gel electrophoreses (SDS-PAGE) with molecular weight 28.18 kDa. The optimal pH and temperature for activity of lipase were 6.4 and 48 °C, respectively, which are higher than those lipases from other penicillium sources. The P. camembertii Thom lipase is 1,3-positional specificity for hydrolysis of triglyceride and hydrolyses plant oil preferentially to animal oil. The lipase can be used in short chain ester synthesis with an esterification degree of 95%. |
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