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Marıa de Lourdes Garcıa-Magana,Julian Gonzalez-Borrayo,Efigenia Montalvo-Gonzalez,Enrique Rudino-Pinera,Sonia G. Sayago-Ayerdi,Jesus Aaron Salazar-Leyva 한국응용생명화학회 2018 Applied Biological Chemistry (Appl Biol Chem) Vol.61 No.4
The aim of this research is the partial characterization of proteases extracted from B. karatas; the isolation and purification of proteases from B. karatas fruits were achieved using precipitation, separation by size exclusion chromatography and anion-exchange chromatography; molecular mass (MM) was determined, and the effect of inhibitors, reducing agents and heat on enzyme activity was analyzed. These proteases were compared with proteases from Bromelia pinguin (B. pinguin) and evaluated under similar conditions. The isolation procedure was adequate; only a few protein bands are present in sodium dodecyl sulfate polyacrylamide gel electrophoresis. Furthermore, zymogram analysis showed protein bands with enzyme activity. Inhibitors, reducing agents and heat were unable to inactivate the proteases extracted from B. karatas and B. pinguin. The semi-purified extracts are a set of proteases with a MM of 66 kDa, but different isoelectric points (3.5–6.5 for B. karatas and 5–9 for B. pinguin), which are found in quaternary structures with proteolytic activity. When denatured, they segment into fragments of approximately 20 and 10 kDa. The data indicate that these plants could be used as sources of proteases since they present good proteolytic activity (21.93 UT for proteases from B. karatas and 43.58 UT for proteases from B. pinguin) and that B. Karatas has potential applications comparable to B. pinguin in the food and health industries.
Meza-Espinoza, Libier,Vivar-Vera, Maria de los Angeles,Garcia-Magana, Maria de Lourdes,Sayago-Ayerdi, Sonia G.,Chacon-Lopez, Alejandra,Becerrea-Verdin, Eduardo M.,Montalvo-Gonzalez, Efigenia 한국식품과학회 2018 Food Science and Biotechnology Vol.27 No.2
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 $37-60^{\circ}C$, similar to Bromelia pinguin proteases. The $K_m$ value of proteases from Bromelia karatas was higher ($253.32{\mu}M$) than that of Bromelia pinguin proteases ($234.94{\mu}M$). 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.