The current methods of producing fatty acid methyl esters involves reacting triglycerides (the substrate) with methanol (the acyl acceptor), catalyzed by a soluble alkaline catalyst, resulting in glycerol as a byproduct. Since the value of glycerol is decreasing, this byproduct is then reacted to form glycerol carbonate derivatives. In this research project, the use of immobilized lipases as catalysts for these types of reactions is being studied. Immobilization of the lipase will allow for easy separation so that the lipase can be reused for multiple reactions. The current focus of the project is to evaluate loading and activity of a Candida rugosa lipase by using glass beads (150-212 µm, 212-300µm, and 425-600µm in diameter), Amberlite® Weakly Basic Anion Exchanger IRA-96, and Dowex® MWA-1 as supports, all containing an amine functional group. Immobilization onto these supports is carried out by physical adsorption and covalent binding. For covalent binding, glutaraldehyde and cyanuric chloride are used as cross-linking agents and are compared for their affect on loading and activity of the lipase. When running reactions, the substrate used is tributyrin and instead of using an alcohol, dimethyl carbonate (DMC) serves as the acyl acceptor. The reasons for using DMC instead of methanol are twofold: 1) Methanol is toxic while DMC is environmentally friendly, and 2) Using DMC forms glycerol carbonate derivatives readily as the byproduct, thus eliminating one step from the current process.