Production and characterization of lipase from Penicillium aurantiogriseum under solid-state fermentation using sunflower pulp

Solid-State Fermentation (SSF) defined as a system in which the growth of microorganisms occurs on a moist solid substrate, shows tremendous potential in applications of microbial enzyme production as a low-cost, low-energy option. In this work, the production of lipase from Penicillium aurantiogriseum by using SSF was investigated. For this purpose, the sunflower pulp, an agro-industrial by-product, was utilized as a solid substrate in the SSF method. The optimization and characterization studies for lipase extract were performed by using the p-nitrophenyl palmitate (pNPP) (C16) as substrate. The lipase activity was found as 29.6 +/- 0.11 U/mg protein at optimum conditions (50 mM of Tris-HCl buffer, pH 7.0, 40 degrees C). In thermal stability assay, the catalytic activities of lipase which are kept at 40, 50 and, 60 degrees C in a water bath for 1 h, were calculated as 100%, 60.48 +/- 1.3%, 32.67 +/- 0.2%, respectively. Also, the enzyme lost rapidly its activity within 15 min at 70 degrees C. The kinetic data, K (m) and V (max) , were determined as 0.17 mM and 2.9 mu M/min, respectively. Also, 10 mM of Ba+2 ion had a slight activating effect (15%) showed on lipase. Lipase kept about 50% of its activity at 4 degrees C at the end of the 30 days. The hydrolytic activities of lipase for commercial olive oil and sunflower oil were found as 3.52 +/- 0.1 U/mg and 3.90 +/- 0.12 U/mg, respectively. The SSF method had obvious potential for the sustainable and cost-effective production of lipase from P. aurantiogriseum. Also, these results confirmed that the sunflower pulp could be used as an alternative substrate to produce enzymes in SSF conditions.

Automated summary

Solid-State Fermentation (SSF) is a promising method for microbial enzyme production on a moist solid substrate. In this study, lipase was produced from Penicillium aurantiogriseum using SSF with sunflower pulp as a solid substrate. The optimized conditions resulted in a lipase activity of 29.6 ± 0.11 U/mg protein, demonstrating the potential for cost-effective enzyme production.