Neutrase® imobilizadada em suportes de quitosana associada a diferentes copolímeros ativados com epicloridrina.

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 5% Saccharomyces cerevisiae. Both supports were activated with epichlorohydrin. The Neutrase® (88ugstand-1) was added to the activated supportand keptunder stirringat 25 °C for 3 h. The active tiesof soluble and immobilized Neutrase® were evaluated by spectrophotometric analysisat 700 nm. The derivatives were analyzed when the yield of immobilization (RI), activity recovered (AREC), half-life (t ½) and thermal stabilization factor (EF),forty-one times greater than theenzyme. The support chitosan 2.5% - 2.5% gelatin IR showed 11% and 64% 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% 71% and 8% of arec presenting FE eighty-six times higher than the soluble enzyme Neutrase ®, the support being chosen as more promising.