| Title | Bacillus licheniformis의 세포막 프로티아제 부분 정제 및 특성 | ||
| Author | 홍난숙 · 최명언 · 양철학 | ||
| Address | 서울대학교 자연과학대학 화학과 | ||
| Bibliography | Korean Journal of Microbiology, 27(3),245-249, 1989 | ||
| DOI | |||
| Key Words | B. licheniformis proteases | ||
| Abstract | Extracellular proteases of Bacillus licheniformis were partially purified using ammonium sulfate fractionation and Sephadex G-75 gel filtration chromatography. The partial purification permited the weparation of two different protease activities, type I and type II. Protease type I is an enzyme with rather high protealytic activity toward dasein and was highly susceptible to organofluoride and EDTA inhibitions. It showed maximal proteolytic activity at pH 7.5 and was rapidly denatured at 71℃. Protease type II is a protease with relatively lower proteolytic activity than the type I. It was also inhibited by 10mM of EDTA and 1mM of PMSF by 30 min incubation. The enzyme showed maximal activity at pH 8.0 and was denatured relatively slowly at 71℃. | ||
| Download PDF | Kor_270312_245-249p.pdf | ||