Purification and properties of a neutral protease produced by Lactobacillus brevis
dc.contributor.author | Amund, Olukayode O. | |
dc.contributor.author | Omidiji, O. | |
dc.date.accessioned | 2019-06-24T13:03:49Z | |
dc.date.available | 2019-06-24T13:03:49Z | |
dc.date.issued | 1990-03-01 | |
dc.description.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. | en_US |
dc.identifier.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. | en_US |
dc.identifier.uri | https://doi.org/10.1016/0168-1656(90)90083-N | |
dc.identifier.uri | http://repository.elizadeuniversity.edu.ng/handle/20.500.12398/123 | |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.subject | Lactobacillus | en_US |
dc.subject | ProteasepH | en_US |
dc.subject | Temperature | en_US |
dc.subject | Cation | en_US |
dc.title | Purification and properties of a neutral protease produced by Lactobacillus brevis | en_US |
dc.type | Article | en_US |
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