Imobilização de Neutrase® em suportes de quitosana associada a diferentes copolímeros.

Abstract

Enzymes are complex structures, and generally fragile adverse conditions may inactivate itself, so the use of immobilization, which is to confine, by chemical and / or physical enzyme in a portion of space, or that is, the enzyme is physically or chemically associated to a support or matrix. The use of the enzyme Neutrase ® is explained to be a protease that hydrolyzes proteins from whey, a by highly polluting and disposed in the dairy industry, in order to obtain derivatives with improved functional properties suitable for the preparation of food for people on diets special or congenital flaws in the protein metabolism. The aim of this work was the production and comparison of media associated with different chitosan copolymers and microorganism. The media used were 2.5% chitosan - gelatin 2.5% and 2.5% chitosan - gelatin 2.5% - 5% Saccharomyces cerevisiae. Both supports were activated with glutaraldehyde. The Neutrase ® (10 U/g stand) was added to the activated support and kept under stirring at 25 ° C for 3 h. The activities of soluble and immobilized Neutrase ® were evaluated by spectrophotometric analysis at 700 nm. The derivatives were analyzed when the yield of immobilization (RI), activity recovered (AREC), half-life (t ½) and thermal stabilization factor (EF), compared with the soluble enzyme. The support chitosan 2.5% - 2.5% gelatin IR showed 36% and 52% of arec presenting FE five hundred fourteen times greater than the soluble enzyme Neutrase ®. And the support chitosan 2.5% - 2.5% gelatin - Saccharomyces cerevisiae IR introduced 5% 76% and 13% of arec presenting FE five hundred thirteen times greater than the soluble enzyme Neutrase ®, the support being chosen as more promising.