Purification and Characterization of An Exocellular Protease of Vibrio Parahaeamoliticus
| Autor: | Shyu,Jia Tzer, 徐嘉澤 |
|---|---|
| Rok vydání: | 1993 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 81 Production of an extracellular protease by a clinical isolate of Vibrio parahaemolyticus (strain ST550) was induced when cultured in iron-limited environment. This protease was partial purified by ammonium sulfate fractionation of the iron-limited culture supernatant, successive ultrafiltration with Diaflo membrane XM50 and YM30, and diethyl-aminoethyl-Sephacel column chromatography. Molecular weight of this partial purified protease was ca. 41,900 by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The optimum pH of the protease was 7.0 to 8.0, and optimum tempereture was 40.degree.C. The V. parahaemoly- ticus protease was inhibited by heat treatment, chymostain and chelating agents. Calcium and/or ferrous ion were essential for its enzyme activity. The protease hadcaseinolytic, elastolytic and collagenolytic activities. Hemolobin was also hydrolysed by this protease, and it suggested that the protease could contri- bute to the efficient utilization of heme by the bacteria, and hence be a virulence factor. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
| Externí odkaz: |
|