Extracellular lipase of Aspergillus niger NRRL3; production, partial purification and properties.

Four strains of Aspergillus niger were screened for lipase production. Each was cultivated on four different media differing in their contents of mineral components and sources of carbon and nitrogen. Aspergillus niger NRRL3 produced maximal activity (325U/ml) when grown in 3% peptone, 0.05% MgSO(4).7H(2)O, 0.05% KCl, 0.2% K(2)HPO(4) and 1% olive oil:glucose (0.5:0.5). A. niger NRRL3 lipase was partially purified by ammonium sulphate precipitation. The majority of lipase activity (48%) was located in fraction IV precipitated at 50-60% of saturation with a 18-fold enzyme purification. The optimal pH of the partial purified lipase preparation for the hydrolysis of emulsified olive oil was 7.2 and the optimum temperature was 60°C. At 70°C, the enzyme retained more than 90% of its activity. Enzyme activity was inhibited by Hg(2+) and K(+), whereas Ca(2+) and Mn(2+) greatly stimulated its activity. Additionally, the formed lipase was stored for one month without any loss in the activity.