Aplicação da microfiltração no processo de obtenção da enzima invertase

Abstract

Enzymes are catalytic proteins widely used in various industrial sectors due to their ability to accelerate chemical reactions. However, obtaining pure and active enzymes from natural sources can be a complex and expensive process. Membrane filtration appears as a promising technique for enzyme separation, offering significant advantages over other conventional techniques. This study aimed to evaluate the performance of different polymeric microfiltration membranes in the purification of the invertase enzyme, originating from the yeast Saccharomyces cerevisiae. The parameters pore diameter (0.22, 0.45, 0.65 and 0.80μm) and transmembrane pressures (1, 2 or 3 Kgf/cm2) were evaluated. The results showed a similar permeate flow behavior, regardless of pore diameter or pressure: rapid decay of the permeate flux with stabilization between 0.067 e 0.083 Kg.h-2.m-2. The formation, practically instantaneous, of a secondary filtration layer on the surface of the membrane was observed, originating from the colloidal material in the enzymatic extract that was not completely removed by centrifugation. The membranes were able to remove colloidal particles, producing a clear extract, with enzymatic activity demonstrated through the sucrose inversion reaction.