Evolução Dirigida da alfa-amilase de Bacillus subtilis

Abstract

Alpha-amylases belongs an enzyme's group who clives a-D-(1,4)-glicosidics bounds in amyloses and amylopectins chains, obtainning small oligosacharides with a alpha-anomeric configuration. That group have a ubiquity distripution in all the three life 's domains, been an important enzyme in carbohidrate metabolic pathway. They have a biotechnologic utilization at the industrial enterprises, who use alpha-amylases from microorganisms sources. Between that alpha-amylases producers, we can cite the Bacillus subtilis specie. That specie is common found in soils, water and association with plants in every world. Member of this genus are known by the special caracteristics of they alpha-amylases, like the thermal stability. The thermostability can be studied by sequence alignment or protein enginnering, like the modelation of altematives primary structures and their influence on the stability. ln this work, we made an alignment between meso- and thermophilics species from both genus Bacillus and Geobacillus and tried to criate enzimatic diversity by using the gene-coding alpha-amylase from B. subtilis. We observed a predominance of hidrophobic/polar aminoacids in thermophilic B. stearothermophilus, showed the importance of enzimatic compactation and consequently inexistence of internai enzymatic spacers, fact that can 't be isolated for the high thermoestability gain.