Esterolytic Activities of Rat Intestinal Mucosa

Abstract
A glycerol-ester hydrolase from rat intestinal cells was purified using chromatography on carboxyhexanoyl-Sepharose-glyceryldioctanoate and preparative gel electrophoresis. The enzyme gave a single band by analytical gel electrophoresis; it was a monomer of 68,000 MW. The optimum pH for its action on glyceryl tributyrate was between 8.0 and 8.5; the activation energy was calculated to be 8.7 kcal .times. mol-1 (36.4 kJ/mol). Its substrate specificity was mainly directed against esters of glycerol and of primary monoalcohols. Similarly to pancreatic lipase but contrary to liver esterase, it was inhibited by bile salts; relief of this inhibition by colipase was only observed for pancreatic lipase. The possible role of the glycerol-ester hydrolase in the absorption of short and of medium chain triglycerides was discussed.

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