The selectivity of the hydrogenation of linseed oil
We have invest igated the se lec t iv i ty of the hydrogenat ion of l inseed oil, which is a mix tu re of t r i g l y c e r ides of fatty acids of different degrees of unsaturat ion linolenic, l inoleic, and ole ic and sa tura ted fatty acids . Depending on the conditions of hydrogenat ing oils and fats , the p roce s s may go according to the following scheme , given in the l i t e r a tu re [1]:
Some additional notes on the kinetics and theory of fatty oil hydrogenation
Summary1.Equations are given for estimating from the composition of oil samples the relative reaction rates of the different unsaturated fatty acids in an oil subjected to catalytic hydrogenation.2.Application of the equations to data from the hydrogenation of cottonseed oil reveals that the ratio of reaction rates, linoleic acid to oleic acid, varies from about 4 to 1 in very non-selective to about 50 to 1 in very selective hydrogenation. Re-examination of analytical data on two series of linseed oils hydrogenated selectively and non-selectively showed the following relative reaction rates for oleic, isolinoleic (9: 10, 15: 16 octadecadienoic), linoleic, and linolenic acids, respectively: non-selective, 1, 2.5, 7.5, 12.5; selective, 1, 3.85, 31, 77. In the non-selective hydrogenation of the oil, 24% of the linolenic acid reacting went to linoleic acid, 65% to isolinoleic acid, and 11% directly to oleic acid. In the selective reaction the corresponding figures were none to linoleic acid, 54% to isolinoleic acid, and 46% to oleic acid. The behavior of soybean oil hydrogenated selectively was quite similar to that of linseed oil.3.The results are discussed in relation to the theory of catalytic hydrogenation. They indicate that the solution of hydrogen in the oil and the adsorption of unsaturated oil on the catalyst are the two steps which are controlling with respect to the reaction rate. It is suggested that the hydrogen pressure, the degree of hydrogen dispersion through the oil, the catalyst concentration, and the temperature all affect the selectivity of the reaction through their influence on the concentration of hydrogen in the reaction zone, with selectivity being favored by a low concentration.
New method for analysis of enzymatic reactions: Thermolysin-catalyzed synthesis of aspartame precursor
Aspartame is an artificial sweetener which is 200 times sweeter than sucrose. A precursor of aspartame, N-(benzyloxycarbonyl)-l-aspartyl-l-phenylalanine methyl ester (Z-APM) was synthesized and hydrolyzed with thermolysin in an aqueous monophasic system. Graphical plotting methods and/or nonlinear regression have been used to analyze enzymatic reactions because of the nonlinearity of enzymatic rate equations. There are, however, problems: the former require accurate measurement of the initial reaction rate and the latter gives no analytical information. The authors proposed a method to solve the nonlinear enzymatic rate equations with respect to the concentration of a product with the Taylor expansion, especially for the reversible Theorell-Chance mechanism (Murakami, Y., Hirata, M., and Hirata, A., J. Ferment. Bioeng., 82, 246–252, 1996). This solution, however, is complex for practical use. In this paper, a simpler solution to explain the thermolysin-catalyzed synthesis of Z-APM is obtained. New methods to determine the kinetic parameters, especially for the reversible Theorell-Chance mechanism, based on the approximated solution are proposed. The results calculated using the obtained kinetic parameters can satisfactorily explain the experimental results, which demonstrates the effectiveness of the proposed analysis. We must know the relation between the concentrations of substrates and a product, and accurately evaluate of the result obtained using Taylor expansion when we determine the kinetic parameters using our newly developed methods. The methods to determine the kinetic parameters of the reversible Theorell-Chance mechanism described in this paper is, however, expected to be applied to general enzymatic reactions.