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http://repository.elizadeuniversity.edu.ng/jspui/handle/20.500.12398/123| Title: | Purification and properties of a neutral protease produced by Lactobacillus brevis |
| Authors: | Amund, Olukayode O. Omidiji, O. |
| Keywords: | Lactobacillus ProteasepH Temperature Cation |
| Issue Date: | 1-Mar-1990 |
| Publisher: | Elsevier |
| Citation: | Amund, O. O., Omidiji, O., & Ilori, O. (1990). Purification and properties of a neutral protease produced by Lactobacillus brevis. Journal of biotechnology, 13(4), 361-365. |
| Abstract: | A proteolytic enzyme was produced by a strain of Lactobacillus brevis isolated from an oriental beverage. The enzyme was extracted and purified 50-fold by gel filtration and ion-exchange chromatography. The optimum pH for the enzyme was 7.0, the optimum temperature 35°C and the molecular weight 34,674 Da. Furthermore, the enzyme was stimulated by cations including Ca2+, Mg2+, Na+ and K+ and inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, ascorbic acid and citric acid. The enzyme is probably a neutral metalloprotease. |
| URI: | https://doi.org/10.1016/0168-1656(90)90083-N http://repository.elizadeuniversity.edu.ng/jspui/handle/20.500.12398/123 |
| Appears in Collections: | Research Articles |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Purification and properties of a neutral protease produced by Lactobacillus brevis.pdf | Abstract | 457.62 kB | Adobe PDF |  View/Open |
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