Abstract
Enterobacter aerogenes Lipase used in this study was heterologously expressed by Pichia pastoris. D152, D152H, D151H, D113, 724), three types of anion resins ( D380, D 301R, D311) and two types of chelating r activities of the immobilized ( EAL). According to the results, D152 was selected for haydrolysis activity as the immobilized enzyme (EAL) . The D152 was selected for hydrolysis activity since the immobilized lipase exhibited the highest specific hydrolysis activity. Immobilization conditions (enzyme loading, immobilization time, temperature, and pH value) . The best results were enzyme loading 4mg/g, time 80min, temperature 30°C, and buffer pH 8; and under the optimized conditions the immobilization efficiency was 95% and the specific activity was 532841.34 U/g.esins (D401, D418) were sieved as support matrix. Hydrolysis assay was employed to evaluate the specific.
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