Enzyme activity and partial characterization of proteases obtained from Bromelia karatas fruit and compared with Bromelia pinguin proteases

The enzymatic activity and partial characterization of proteases from Bromelia karatas fruits were evaluated and compared with Bromelia pinguin proteases. The specific activity increased twofold after partial purification in both proteases. Partially purified proteases from Bromelia karatas showed good specific activity at pH 6.0–8.0 and residual activity of 70–100% for 60 min at 37–60 °C, similar to Bromelia pinguin proteases. The K m value of proteases from Bromelia karatas was higher (253.32 µM) than that of Bromelia pinguin proteases (234.94 µM). The use of specific protease inhibitors indicated the presence of cysteine and serine proteases. Proteases with molecular weight of 66.2–97 and 21–31 kDa were detected. Bromelia karatas proteases registered 73% hydrolysis using a soy protein concentrate, similar to the enzyme activity of Bromelia pinguin proteases and commercial bromelain. These results demonstrate that Bromelia karatas proteases could be a potential alternative protease in the food industry.