| | 1 | Author
| M. O. Ilori, O. O. Amund, O. Omidiji | Requires cookie* | | | Title
| Characterisation of a Neutral Protease Produced by Micrococcus luteus  | | | | Abstract
| A proteolytic enzyme produced by a cassava-ferment ing strain of Micrococcus luteus was extracted and puri fied 50-fold by gel filtration and ion exchange chroma tography. The optimum pH for the enzyme was 7.0, the opti mum temperature 25 °C, the apparent molecular weight 42 kDa and the K m value, 0.45 mg m l-1 with casein as substrate. The enzyme was stimulated by Ca2+ and Mg2+ but inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, KCN, citric acid and L-cysteine indicating the enzyme to be a metalloprotease. | | | |
Reference
| Z. Naturforsch. 51c, 429—431 (1996); received May 26 1995/January 15 1996 | | | |
Published
| 1996 | | | |
Keywords
| M etalloprotease Purification, Heat Inactivation, Apparent Molecular Weight, Inhibitors | | | |
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| default:Reihe_C/51/ZNC-1996-51c-0429_n.pdf | | | | Identifier
| ZNC-1996-51c-0429_n | | | | Volume
| 51 | |
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