Lipolytic Activity of Syncephalastrum racemosum

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Abstract
Lipase from S. racemosum was recovered by ammonium sulfate precipitation and gel filtration on Sephadex G-75. Maximum lipase activity was observed at pH 6.0 and 37.degree. C. Among various synthetic triglycerides, tributyrin was hydrolyzed in preference to the others, whereas butter oil was degraded most among natural triglycerides. Salts of Na and Ca stimulated lipase activity, but salts of Cu, Fe, Li and Zn were inhibitory. Chemical agents like mercuric chloride, potassium permanganate, p-chloromercuribenzoate and sodium lauryl sulfate brought about inhibition of lipase activity. The enzyme was inactivated completely at 60.degree. C after 15 min.