Fernanda S. Medeiros, Marina Marcuschi, Caio Rodrigo Dias de Assis, Janilson Felix da Silva, Talita da Silva Esposito, Ranilson de Souza Bezerra
Alkaline proteases from the intestine of mutton snapper (Lutjanus analis) were partially purified via a three-step process. The enymes exhibited tryptic specific activity 13.7-fold higher than that of crude extract, with a 10% purification yield, and were strongly inhibited by TLCK, benzamidine, and PMSF. These proteases were stable at temperatures up to 55°C and were most active within a pH and temperature range of 8.0-11.5 and 50-60°C, respectively. These enzymes exhibited high affinity to BApNa substrate, with the Km and Vmax values of 0.56 ± 0.14 and 0.609 ± 0.05 U/min, respectively. Mutton snapper proteases were more active than commercial porcine trypsin in the presence of surfactants such as Triton X-100, Tween 20, Tween 80, and Extran®. In addition, the mutton snapper protease was stable with hydrogen peroxide and commercial detergents. These results demonstrate that these proteases have a potential for application in the detergentindustry.
