Abstract
An enzyme preparation from human skim milk, enriched in bile salt-stimulated lipase activity, but devoid of serum-stimulated lipase activity, was active against both emulsified, water-insoluble substrates (trioleylglycerol and tributyrylglycerol) and a water-soluble substrate ( p-nitrophenyl acetate). Bile salt was a prerequisite for activity against emulsified trioleylglycerol but not for activity against emulsified tributyrylglycerol or p-nitrophenyl acetate although bile salt enhanced the activity several-fold also against these substrates. The enzyme was stable in milk and in buffer solution but was rapidly inactivated in the presence of emulsified triacylglycerols. Bile salt protected the enzyme from this inactivation. Bile salt caused a more than 10-fold increase of the maximal reaction rate when p-nitrophenyl acetate was the substrate. The decrease of K m was less pronounced. During the hydrolysis of emulsified trioleylglycerol there was a rapid release of glycerol, and glycerol and free fatty acids were the major products formed during the reaction.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
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