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• W2899481134 abstract "Pichia pastoris expression is a mature and efficient eukaryotic expression system. In this work, Aspergillus oryzae lipase (AOL, with the molecular mass of 28 kDa), which can perform highly stereoselective hydrolysis of (R, S)-methyl 2-(4-hydroxyphenoxy) propanoate, was expressed in P. pastoris X-33. The specific activity of AOL was 432 U/mg, which was obtained by fed-batch cultivation in a 5 L bioreactor using a methanol feeding strategy. After fermentation, the supernatant was concentrated by ultrafiltration with a 10 kDa cut-off membrane and purified with DEAE-Sepharose™ FF ion-exchange chromatography and phenyl Seflnose™ 6 FF hydrophobic interaction chromatography. The purified lipase activity reached 5509 U/mg. AOL showed high activity toward short-chain triacylglyceride (C4), and the optimum temperature and pH were 40 °C and 8.0, respectively. The purified enzyme activity was inhibited by Zn2+ and Cu2+. Moreover, the Km and Vmax values were 1 mM and 32.89 mmol/min, respectively." @default.
• W2899481134 created "2018-11-09" @default.
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• W2899481134 date "2019-03-01" @default.
• W2899481134 modified "2023-10-08" @default.
• W2899481134 title "High-level expression and characterization of a stereoselective lipase from Aspergillus oryzae in Pichia pastoris" @default.
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• W2899481134 doi "https://doi.org/10.1016/j.pep.2018.10.012" @default.
• W2899481134 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30389593" @default.
• W2899481134 hasPublicationYear "2019" @default.
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