Enhanced Production of Penicillium expansum PED-03 Lipase through Control of Culture Conditions and Application of the Crude Enzyme in Kinetic Resolution of Racemic Allethrolone

Abstract

Alkaline lipase production was performed in submerged fermentation by Penicillium expansum PED-03. It was found that the suitable carbon source and nitrogen source for lipase production were 0.5% starch and 4.0% soybean meal, respectively. The maximal lipase activity (850 U/mL) of production was achieved at initial pH 5.5-6.0, 26 degrees C, 72 h. Tween-80 was an effective enhancer for lipase production. Agitation speed of the fermentor played an important role, and the suitable agitation speed for lipase production was 500 r/min. The lipase was stable within the range of pH 7.0-10.0 and 20-40 degrees C, and the optimum conditions for the enzymatic reaction were 35 degrees C and pH 9.5. The enzymatic resolution of racemic allethrolone (4-hydroxy-3-methyl-2-(2-propenyl)-2- cyclopenten-1-one) was carried out by the lipase from P. expansum PED-03, and the conversion reached 48% with excellent enantioselectivity (E > 100), which showed a good application potential in the production of optically pure allethrolone.

Production of extracellular lipases by Rhizopus oligosporus in a stirred fermentor

“…Effect of the gradual increase in impeller speed has also been investigated that ranges between 400-900 rpm (5). For this purpose, scale up studies in a laboratory scale stirred fermenter for extracellular lipase production from selected mutant strain was subsequently evaluated in parallel with wild strain.…”

Characterization of the 5′ flanking region of lipase gene from Penicillium expansum and its application in molecular breeding

“…Three decades ago, a filamentous fungus, Penicillium expansum , was isolated from soil as a productive producer of alkaline lipase . Subsequently, several strategies were applied to maximize the productivity of P. expansum lipase (PEL), including traditional mutation breeding , fermentation process optimization , and heterologous expression . After several years of mutation breeding accompanied by fermentation process optimization, the commercial production of PEL was achieved and its products are widely applied as an important additive in the leather and detergent industries (http://www.leveking.com) to increase the degreasing efficiency.…”

Molecular cloning and characterization of the glyceraldehyde-3-phosphate dehydrogenase gene from Penicillium expansum PE-12

“…Penicillium expansum is of considerable importance from a biotechnological aspect as a consequence of its content of versatile lipase (Dai and Xia, 2005). The lipase secreted by P. expansum (called PEL) can effectively hydrolyze the 3 ester bonds of triacylglycerol under alkaline condition (Bian et al, 2005) and is therefore widely used in laundry detergent and leather industry (www.leveking.com).…”

“…However, back to the first discovery of PEL, the lipase productivity of this species was rather low, which made it impractical for commercial production (Stocklein et al, 1993). Later on, several strategies were adopted to maximize the production level of PEL including successive mutagenesis and selection (Zhang et al, 2001), fermentation condition optimization (Dai and Xia, 2005), and heterologous expression (Yuan et al, 2003;Zhang et al, 2010). After 2 decades of mutagenesis and selection accompanied by fermentation condition optimization, the industrial production of PEL was realized.…”