Ranyere Lucena de Souza, José Murillo P Barbosa, Gisella Maria Zanin, Marcos Wandir N Lobão, Cleide Mara F Soares, Alvaro Silva Lima
Universidade Tiradentes, Av. Murilo Dantas, 300, Prédio do ITP, Farolândia, 49032-490 Aracaju-Sergipe, Brazil.
Applied biochemistry and biotechnology 2010 MayThe hydrolysis of triglycerides at the oil-water interface, synthesis of esters and transesterification in microaqueous conditions are catalysed by lipase. For its application, a proper purification method was necessary. This study examined the application of an aqueous two-phase system to partition porcine pancreatic lipase. The influence of molecular weight and concentration of polyethylene glycol (PEG), tie line length (TLL), potassium phosphate concentration, sodium chloride (NaCl) addition and temperature in the partition was studied. The enzyme was more efficiently purified in PEG 8,000 at 14.5 degrees C (PF = 3.89-fold), presenting more recoveries at the top phase with shorter TLL and lower concentrations of PEG and potassium phosphate. Moreover, the increase of these variables repressed the purification and the further addition of NaCl did not promote the purification of the enzyme. These results demonstrated the efficiency of the aqueous two-phase system on lipase purification.
Ranyere Lucena de Souza, José Murillo P Barbosa, Gisella Maria Zanin, Marcos Wandir N Lobão, Cleide Mara F Soares, Alvaro Silva Lima. Partitioning of porcine pancreatic lipase in a two-phase systems of polyethylene glycol/potassium phosphate aqueous. Applied biochemistry and biotechnology. 2010 May;161(1-8):288-300
PMID: 20119857
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