Abstract
Patel, Virendra (University of Missouri, Columbia), Herbert S. Goldberg, and Donald Blenden. Characterization of leptospiral lipase. J. Bacteriol. 88:877–884. 1964.—A technique for leptospiral lipase extraction which yielded a highly active, stable, and concentrated lipase preparation was developed. The chief characteristics of leptospiral lipase were determined and are summarized below. Leptospiral lipase was soluble in water and stable in both the dry state and in aqueous solution. Tributyrin was found to be the substrate upon which the enzyme was most active. With this substrate, leptospiral lipase was found to display optimal activity at pH 7 and at 30 C. The Michaelis constant of leptospiral lipase with tributyrin substrate was determined to be 4.76 × 10-2m. The enzyme was not inhibited by low concentrations of mercury, iron, cobalt, or copper or by —SH blocking agents. Bile and calcium chloride in low concentrations were able to increase lipase activity at alkaline pH. The isoelectric point of leptospiral lipase was determined to be in the range of pH 5.2 to 5.4.
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Selected References
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