Immobilization of a recombinant esterase from Lactobacillus plantarum on polypropylene Accurel MP1000.
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.
Kolling
Deise Juliana
DJ
Departamento de Ciência e Tecnologia de Alimentos, Universidade Federal de Santa Catarina, Florianópolis, Brazil.
Suguino
Willian Alexandre
WA
Brod
Fábio Cristiano Angonesi
FC
Arisi
Ana Carolina Maisonnave
AC
D000327:Adsorption; D002087:Butyrates / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli; D004950:Esterases / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D006863:Hydrogen-Ion Concentration; D048191:Lactiplantibacillus plantarum / Q000201:enzymology; D011126:Polypropylenes / Q000737:chemistry; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*; D013696:Temperature
D002087:Butyrates; D004800:Enzymes, Immobilized; D011126:Polypropylenes; D011994:Recombinant Proteins; C033592:4-nitrophenyl butyrate; D004950:Esterases