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BY-NC-ND 3.0 license Open Access Published by De Gruyter June 2, 2014

Characterisation of a Neutral Protease Produced by Micrococcus luteus

  • M.O. Ilori , O.O. Amund and O. Omidiji

Abstract

A proteolytic enzyme produced by a cassava-ferment­ing strain of Micrococcus luteus 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 25 °C, the apparent molecular weight 42 kDa and the Km value, 0.45 mg ml-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.

Received: 1995-5-26
Revised: 1996-1-15
Published Online: 2014-6-2
Published in Print: 1996-6-1

© 1946 – 2014: Verlag der Zeitschrift für Naturforschung

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

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