STABILIZATION OF MICROBIAL ENZYMATIC PREPARATIONS USED IN FEED INDUSTRY

Abstract

The enzymatic compound with protease activity obtained by Bacillus licheniformis CMIT 1.33 cells fermentation was entrapped in sol-gel matrixes, using TEOS as precursor. The sol-gel technique is a soft method for silica glass synthesis at room temperature. In silica gels, the enzymes maintain their catalytic activity for a longer period of time and present high stability at environmental factors. Bacillus licheniformis CMIT 1.33 enzyme was also immobilized by entrapment in silica gels deposited on a ceramic support. The optimal temperature and pH of the native and immobilized enzyme did not vary significantly. At temperature and pH values lower than the optimum, the relative activities have been higher for the immobilized compound. The immobilization of the enzymatic compound increased the stability. The enzymatic compounds with protease activity obtained by silica gels entrapment and entrapment/deposition on ceramic support can be used as forage additive.