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Improved Stabilities of Lipase by Immobilization on Eupergit C

机译:通过对eupergit C的固定化改善脂肪酶的稳定性

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Lipase is frequently used for catalyze wide non-natural substrates in order to obtain enantio- and regioselectivie substrates. This study evaluates the stabilities of lipase by immobilization on Eupergit C. The immobilized lipase had improved stability at 60 ° C for 60 h compared to the free lipase 1 h at 60 ° C. Immobilization resulted in an increase in pH stability over a range of 7.0 - 9.0 and about 54 days for half-life of storage at 4 ° C. The tolerance of lipase to organic solvents was also improved by immobilization, and the immobilized lipase showed activating activity when exposed to hydrophobic solvents.
机译:脂肪酶经常用于催化宽的非天然基底以获得对enaNIO和enfioSelectivie底物。该研究评估脂肪酶对Eupergit C的稳定性。与60℃下的游离脂肪酶1 H相比,固定化脂肪酶在60℃下在60℃下提高稳定性。在60℃下固定导致pH稳定性的增加导致了一系列的pH稳定性7.0 - 9.0和约54天的储存在4℃下的半衰期。通过固定化也改善了脂肪酶对有机溶剂的耐受性,并且在暴露于疏水性溶剂时,固定化脂肪酶在激活活性。

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