High impact information on Tricaproylglycerol

• The observed striking inhibitory effect (99%) of albumin on the LPL-catalyzed hydrolysis of trihexanoylglycerol is probably the result of the high affinity interaction of albumin with this substrate [1].
• Spectrophotometric analyses indicated that there is one high affinity binding site per albumin molecule (apparent KD = 1.8 +/- 0.9 microM) for the interaction with trihexanoylglycerol [1].
• Weanling male Sprague-Dawley rats were fed purified test diets containing 8% of one of 10 test triglycerides (either tributyrin, tricaproin, tricaprylin, tricaprin, trilaurin, trimyristin, tripalmitin, tristearin, triolein, trilinolein) or corn oil (a mixed triglyceride) for 23 d after an initial 1-wk stabilization period [2].
• The optimum pH and temperature were 6.0 and 37 degrees C. LST-03 lipase was stable at pH 5-8 and below 40 degrees C. Its hydrolytic activity was highest against tricaproin (C6), methyl octanoate (C8), and coconut oil respectively among the triacylglycerols, fatty acid methyl esters, and natural oils investigated [3].
• The lipase showed higher lipolytic activity toward tricaproin (C6) and tricaprylin (C8) among the triacylglycerols examined and preferentially hydrolyzed ester bond of 1- and 3-position of triolein [4].

Gene context of Tricaproylglycerol

• The lipases of both fungal species were most active at a pH of 5.6 and a temperature of 45 degrees C. The best glyceride for assaying the lipase activities of these fungi was trihexanoin while palm oil was a better vegetable oil than the conventional groundnut oil used for the same purpose [5].

References