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• W2886435238 abstract "An active recombinant human pancreatic lipase (recHPL) was successfully prepared for the first time from the Escherichia coli expression system using short Strep-tag II (ST II). The recHPL-ST II was solubilized using 8 M urea from E.coli lysate and purified on a Strep-Tactin-Sepharose column. After refolding by stepwise dialyses in the presence of glycerol and Ca2+ for 2 days followed by gel filtration, 1.8-6 mg of active recHPL-ST II was obtained from 1 L of culture. The recHPL was non-glycosylated, but showed almost equal specific activity, pH-dependency and time-dependent stability compared to those of native porcine pancreatic lipase (PPL) at 37°C. However, the recHPL lost its lipolytic activity above 50°C, showing a lower heat-stability than that of native PPL, which retained half its activity at this temperature." @default.
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• W2886435238 date "2018-08-08" @default.
• W2886435238 modified "2023-10-16" @default.
• W2886435238 title "A novel protocol for the preparation of active recombinant human pancreatic lipase from<i>Escherichia coli</i>" @default.
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• W2886435238 doi "https://doi.org/10.1093/jb/mvy067" @default.
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