Abstract
Lipase from Syncephalastrum racemosum was recovered by ammonium sulphate precipitation and gel filtration on Sephadex G–75. Maximum lipase activity was observed at pH 6.0 and 37°C. Among various synthetic triglycerides, tri-butyrin was hydrolyzed in preference to the others, whereas butter oil was degraded most among natural triglycerides. Salts of sodium and calcium stimulated lipase activity, but salts of copper, ferric, lithium, and zinc were inhibitory. Chemical agents like mercuric chloride, potassium permanganate, p-chloromer-curibenzoate, and sodium lauryl sulphate brought about inhibition of lipase activity. The enzyme was inactivated completely at 60°C after 15min.
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