http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Idalia Osuna-Ruiz,Marı´a Fernanda Espinoza-Marroquin,Jesu´ s Aaro´n Salazar-Leyva,Emyr Pen˜a,Carlos Alfonso A ´ lvarez-Gonza´lez,Isaura Ban˜uelos-Vargas,Emmanuel Martı´nez-Montan˜o 한국식품과학회 2019 Food Science and Biotechnology Vol.28 No.6
Pepsin from stomach of Bagre panamensis wassemi-purified and biochemically characterized. The acidproteolytic activity and purification fold were 3875 U/mgprotein and 91.85, respectively, after purification process. The optimum pH and temperature for semi-purified proteasewere 2–3 and 65 C, respectively. The enzymeactivity was stable after heating proteases at 50 C for120 min, but only 30% residual activity was detected afterheating at 65 C for 30 min. SDS-PAGE analysis showedtwo proteins bands after dialysis (26.1 and 38.6 kDa). Onlythe band of 38.6 kDa had proteolytic activity, which wasinhibited using pepstatin A. Organic solvents, surfactantsand reducing agents affect the proteolytic activity at differentextent; however, metal ions or EDTA have noimpact on protease activity. The semi-purified proteaseexhibited milk coagulant activity, with a maximum activityat 45 C. The obtained results highlight the potentialbiotechnological use of B. panamensis pepsin.