Purification and properties of a neutral protease produced by Lactobacillus brevis

Please use this identifier to cite or link to this item: http://repository.elizadeuniversity.edu.ng/jspui/handle/20.500.12398/123

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DC Field	Value	Language
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.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/jspui/handle/20.500.12398/123	-
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.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
Appears in Collections:	Research Articles

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