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• W2000902017 abstract "The extracellular lipase gene from Yarrowia lipolytica (YlLip2) was cloned into the pPICZαA and integrated into the genome of the methylotrophic yeast Pichia pastoris X-33. The lipase was successfully expressed and secreted with an apparent molecular weight of 39 kDa using Saccharomyces cerevisiae secretion signal peptide (α-factor) under the control of the methanol inducible promoter of the alcohol oxidase 1 gene (AOX1). The lipase activity of 12,500,000 U/l (2.10 g total protein and 0.63 g lipase per liter) was obtained in a fed-batch cultivation, where methanol feeding was linked to the dissolved oxygen content after initial glycerol culture. After fermentation, the supernatant was concentrated by ultrafiltration with a 10 kDa cut off membrane and purified with ion exchange chromatography using Q Sepharose FF. Deglycosylation showed that the recombinant lipase is a glycoprotein which contains the same content of sugar (about 12%) as the native lipase from Y. lipolytica. The optimum temperature and pH of the recombinant lipase was 40 °C and 8.0, respectively. The lipase showed high activity toward long-chain fatty acid methyl esters (C12–C16)." @default.
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• W2000902017 date "2007-06-01" @default.
• W2000902017 modified "2023-10-16" @default.
• W2000902017 title "High-level expression of extracellular lipase Lip2 from Yarrowia lipolytica in Pichia pastoris and its purification and characterization" @default.
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• W2000902017 doi "https://doi.org/10.1016/j.pep.2006.10.018" @default.
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