Pepsin from stomach of Bagre panamensis was semi-purified and biochemically characterized. The acid proteolytic activity and purification fold were 3875 U/mg protein and 91.85, respectively, after purification process. The optimum pH and temperature for semi-purified protease were 2–3 and 65 °C, respectively. The enzyme activity was stable after heating proteases at 50 °C for 120 min, but only 30% residual activity was detected after heating at 65 °C for 30 min. SDS-PAGE analysis showed two proteins bands after dialysis (26.1 and 38.6 kDa). Only the band of 38.6 kDa had proteolytic activity, which was inhibited using pepstatin A. Organic solvents, surfactants and reducing agents affect the proteolytic activity at different extent; however, metal ions or EDTA have no impact on protease activity. The semi-purified protease exhibited milk coagulant activity, with a maximum activity at 45 °C. The obtained results highlight the potential biotechnological use of B. panamensis pepsin.

巴格里巴格纳胃中的胃蛋白酶经过半纯化和生化鉴定。纯化后的酸蛋白水解活性和纯化倍数分别为3875 U / mg蛋白和91.85。半纯化蛋白酶的最佳pH和温度分别为2-3和65°C。将蛋白酶在50°C加热120分钟后，酶的活性稳定，但是在65°C加热30分钟后仅检测到30％的残留活性。SDS-PAGE分析显示透析后有两个蛋白带（26.1和38.6 kDa）。胃蛋白酶抑制剂pepstatin A只能抑制38.6 kDa的条带。有机溶剂，表面活性剂和还原剂在不同程度上影响蛋白水解活性。但是，金属离子或EDTA对蛋白酶活性没有影响。半纯化的蛋白酶具有乳凝活性，在45°C下具有最大活性。获得的结果突出了生物技术在生物技术方面的潜在用途。B. panamensis胃蛋白酶。