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Journal of Lipid Research, Vol. 3, 99-105, January 1962
Copyright © 1962 by Lipid Research, Inc.

The acid lipase of the castor bean. Properties and substrate specificity

Robert L. Ory , Allen J. St. Angelo , and Aaron M. Altschul

Seed Protein Pioneering Research Laboratory, Southern Utilization Research and Development Division, Agricultural Research Service, U.S. Department of Agriculture, P.O. Box 19687, New Orleans 19, Louisiana

A castor bean lipase with a pH optimum of 4.3 is found within the fatty layer obtained by centrifuging a homogenate of the bean; most of the fat may be removed by extraction with ethyl ether in the presence of saturated sodium chloride solution, yielding a preparation which consists of about 55% protein and 5% lipid and which is insoluble in neutral buffer. This preparation emulsifies triglycerides and hydrolyzes them completely; the enzyme is inhibited by mercurials but not by diisopropylfluorophosphate. The data on effect of enzyme concentration on hydrolysis rate suggest that a second component, perhaps an emulsifier, is required for activity. Hydrolysis of triglycerides of saturated fatty acids is maximum at a chain length between C₄ and C₈. Triacetin is not hydrolyzed. Glycerides of long-chain fatty acids, predominantly unsaturated C₁₈, are also hydrolyzed, but not as rapidly as the maximum for the glycerides of short-chain fatty acids. Mono- and dibutyrin are hydrolyzed less rapidly than tributyrin, but diolein is hydrolyzed more rapidly than triolein; this suggests that there may be two separate enzymes for the short-chain and long-chain triglycerides, respectively. Esters of ricinoleic acid and monohydric alcohols are hydrolyzed at a much lower rate than is castor oil.

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