Purification and Properties of a Chromobacterium Lipase with a High Molecular Weight |
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Authors: | Mamoru Sugiura Masakazu Isobe Noriyuki Muroya Tsutomu Yamaguchi |
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Affiliation: | Tokyo College of Pharmacy, Uenosakuragi, Taito-ku, Tokyo |
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Abstract: | A lipase with a high molecular weight was purified from Chromobacterium viscosum by chromatography using the Amberlite CG–50 and Sephadex G–75. The purified lipase (Lipase A) was found to be homogeneous by disc electrophoresis.Lipase A had an optimum pH around 7 for lipolysis of olive oil and the enzyme was stable at the range of pH 4 to 9 and below 50°C. Zn2+, Cu2+, Fe3+ and high concentrations of l-cysteine, iodoacetic acid and NBS had remarkable inhibitory effects. Bile salts were activator. Lipase A was more active on water insoluble esters than water soluble esters. The isoelectric point of the enzyme was pH 4.7. |
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Keywords: | lactic acid bacteria Enterococcus faecium bacteriocin enterocin inducing peptide |
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