Enterobacter aerogenes Lipase immobilized on ion exchange resin D152 as a supportive carrier
DOI:
https://doi.org/10.37376/asj.vi5.4130Keywords:
Enzymatic Properties Enterobacter aerogenes Lipase (EAL, ion exchange resin D152, Immobilization, Hydrolysis, Biotechnology, lipases, Immobilization efficiency, lipase activity recoveryAbstract
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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