Immobilization of a recombinant esterase from Lactobacillus plantarum on polypropylene Accurel MP1000

Deise Juliana Kolling, Willian Alexandre Suguino, Fábio Cristiano Angonesi Brod, Ana Carolina Maisonnave Arisi
Applied Biochemistry and Biotechnology 2011, 163 (2): 304-12
A recombinant esterase from Lactobacillus plantarum was immobilized on hydrophobic support polypropylene Accurel MP1000 by adsorption. Adsorption efficiency was 83%, and the immobilized protein was 12.4 mg/g of support. Esterase activity was determined using p-nitrophenyl butyrate as substrate, and highest activities were observed at 50 °C for immobilized enzyme and 30 °C for free enzyme extract. Concerning thermal stability, after enzyme incubation at 80 °C for 30 min, immobilized and free enzyme retained 91% and 56% of initial activity, respectively. Immobilized enzyme presented lower V(max) and higher K(m) than free enzyme. Protein was not released from the support, and esterase activity increased after 3 cycles of reuse.

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