期刊
JOURNAL OF NUTRITIONAL BIOCHEMISTRY
卷 12, 期 4, 页码 219-224出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/S0955-2863(00)00156-X
关键词
alpha-tocopheryl acetate; alpha-tocopheryl succinate; alpha-tocopheryl nicotinate; pancreatic enzymes; carboxyl ester hydrolase; Michaelis-Menten kinetic
The objective of this study was to examine the in vitro hydrolysis of vitamin E esters (alpha -tocopheryl acetate, alpha -tocopheryl succinate and alpha -tocopheryl nicotinate) by pancreatic carboxyl ester hydrolase (CEH) at the concurrent presence of different bile acids at different concentrations. The assay was performed by measuring the amount of alpha -tocopherol released by porcine pancreatic juice upon addition to different solutions of alpha -tocopheryl esters, which were dispersed in bile acid mixed micelles at 37 degreesC, pH 7.4. The CEH activity was 10 U in the final assay, and the optimal concentration of cholate in this in vitro-system was determined to 30 mM for the hydrolysis of alpha -tocopheryl acetate. The hydrolysis of alpha -tocopheryl esters required presence of pancreatic juice and bile acids, and the results showed furthermore that the ability of pancreatic CEH towards hydrolysis of different alpha -tocopheryl esters increased with increasing lipophility, irrespective of the type or concentration of bile acid present in the assay. Likewise, retinyl palmitate was hydrolyzed at a faster rate than retinyl acetate. The structure of the bile acid influenced the rate of hydrolysis. Thus, cholate followed by glycodeoxy- and glycochenode-oxycholate were the most effective activators of CEH among the bile acids tested in this assay. The presence of gamma -tocopherol or all-trans-retinyl acetate in the assay showed a non-competitive inhibition of the hydrolysis rate of alpha -tocopheryl acetate. (C) 2001 Elsevier Science inc. Ail rights reserved.
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