Evaluation of Porcine and Aspergillus oryzae α-Amylases as Possible Model for the Human Enzyme

α-amylases are ubiquitous enzymes belonging to the glycosyl hydrolase (GH13) family, whose members share a high degree of sequence identity, even between distant organisms. To understand determinants catalytic activity throughout evolution, and investigate use homologous as model for human one, we compared salivary α-amylase, Aspergillus oryzae α-amylase pancreatic porcine using combination in vitro silico approaches. Enzyme sequences were aligned, structures superposed, whereas kinetics spectroscopically studied by commercial synthetic substrates. These three show strikingly different activities, specifically mediated ions, despite relevant structural homology. Our study confirms that function evolution has considerably diverged, although key determinants, such triad calcium-binding pocket, have been retained. functional differences need be carefully considered when α-amylases, from organisms, used enzymes. In this frame, particular focus is needed setup proper experimental conditions.