Enzymatic Modification of Triglycerides

Deuteration Network Members Involved: ESS, STFC

Project Description: The aim of this project is to modify triglycerides by selectively replacing fatty acid tails with deuterated analogues using enzymatic catalysis – specifically, using lipase enzymes. Lipases are the enzymes responsible for the digestion of triglycerides and function by catalysing the hydrolysis of triglycerides to monoglycerides and fatty acids. They can also be manipulated to perform the hydrolysis reaction in reverse – esterifying the hydroxy groups of glycerides. The benefit to using enzymes in place of chemical catalysts is that they often exhibit regioselectivity. Many lipases, for instance, show selectivity for the 1/3-position of triglycerides (Figure 1).

triglyceride 13 reaction
Figure 1. Action of a 1,3-selective lipase on a triglyceride

The chemical deuteration laboratory at ESS is establishing conditions for the enzymatic modification of triglycerides such as triolein, using commercially available immobilised lipases and unlabelled fatty acids. The deuteration laboratory at STFC, with experience in synthesising deuterated fatty acids, have produced palmitic acid-d31 and stearic acid-d35 to be utilised once robust conditions have been established.