Mida H Mayel*, Charles O Nwuche, Vincent Sunday Chimaobi, Sabinus Oscar O Eze and Chilaka FC
Lipases are enzymes with potential industrial applications but their supply is not sufficient for efficient utilization. The present work focused on lipase from two fungal isolates (Aspergillus niger LC 269109 and Aspergillus nidulans). The effects of pH, temperature and substrate concentration on lipase activity, as well as some kinetic parameters were determined. The lipase from Aspergillus nidulans was optimally active at pH 7 and temperature of 40°C, while the lipase from Aspergillus niger LC 269109 was found to be optimally active at pH 6 and temperature of 50°C. Lipase from Aspergillus nidulans was found to have a larger Km (17.54 mg/ml) than the lipase from Aspergillus niger LC 269109 (9.71 mg/ml) and a higher Vmax (769. 23 µmol/min) compared to that of lipase from Aspergillus niger LC 269109 (714.29 µmol/min). Hence, these isolates of Aspergillus nidulans as well as the Aspergillus niger, LC 269109 may be exploited as cheap source of lipase.
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