11^th World Microbiology & Immunology Congress

Biography

Biography: Roberto Fernandez-Lafuente

Abstract

Coimmobilization of enzymes is an increasing topic in biocatalysis It has can save the lag-time that produce the use of enzymes independently immobilized in different particle in casdae reactions. In some cases, is fully compulsory to prevent the destruction of one of the substrates ^. However, there some problems directly related to the fact of coimmobilizing two enzymes in one particle . First, it is possible that the best immobilization protocol differs from one enzyme to the other, making necessary to reach compromise solutions. This makes that immobilization cannot be fully utilized to get improved preparations of both enzymes, losing positive impacts in the biocatalyst design . Second, after inactivation of the least stable enzyme, both enzymes need to be discarded, even if the other enzyme remains fully active.

Here we presented a solution to these problems when one enzyme may be stabilized via immobilization, while the other cannot, and the first immobilized/stabilized enzyme is much more stable than the other enzyme . Using as model enzymes a galactosidase and lipases, we will show how we can coat the immobilized/stabilized lipase, then coat the lipase with PEI and finally immobilize the galactosidase. When the galactosidase is inactivated, the lipases remain almost fully active, that way using high buffer concentration the galactosidase may be released . To prevent the PEI release, we have attached it to the enzyme (using glutaraldehyde) and the support (using glyoxyl-octyl) . This way, several cycles of lipase reuse after galactosidase inactivation could be performed.