Purification and properties of a neutral protease produced by Lactobacillus brevis

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dc.contributor.authorAmund, Olukayode O.
dc.contributor.authorOmidiji, O.
dc.date.accessioned2019-06-24T13:03:49Z
dc.date.available2019-06-24T13:03:49Z
dc.date.issued1990-03-01
dc.description.abstractA 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.citationAmund, 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.urihttps://doi.org/10.1016/0168-1656(90)90083-N
dc.identifier.urihttp://repository.elizadeuniversity.edu.ng/handle/20.500.12398/123
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectLactobacillusen_US
dc.subjectProteasepHen_US
dc.subjectTemperatureen_US
dc.subjectCationen_US
dc.titlePurification and properties of a neutral protease produced by Lactobacillus brevisen_US
dc.typeArticleen_US
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