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1996 (1)
1Author    M. O. Ilori, O. O. Amund, O. OmidijiRequires 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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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0429_n.pdf 
 Identifier    ZNC-1996-51c-0429_n 
 Volume    51