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Natural enzymes are powerful catalysts, reducing the apparent activation energy for reaction, enabling chemistry to proceed as much as 1015 times faster than the corresponding solution reaction. It has been suggested for some time that in some cases quantum tunneling can contribute to this rate enhancement by offering pathways through a barrier inaccessible to activated events. A central question of interest to both physical chemists and biochemists is the extent to which evolution introduces below the barrier or tunneling mechanisms. In view of the rapidly expanding chemistries for which artificial enzymes have now been created, it is of interest to see how quantum tunneling has been used in these reactions. In this paper, we study the evolution of possible proton tunneling during C-H bond cleavage in enzymes that catalyze the Morita-Baylis-Hillman (MBH) reaction. The enzymes were generated by theoretical design followed by laboratory evolution. We employ classical and centroid molecular dynamics approaches in path sampling computations to determine if there is a quantum contribution to lowering the free energy of the proton transfer for various experimentally generated protein and substrate combinations. This data is compared to experiments reporting on the observed kinetic isotope effect (KIE) for the relevant reactions. Our results indicate modest involvement of tunneling when laboratory evolution has resulted in a system with a higher classical free energy barrier to chemistry (that is when optimization of processes other than chemistry result in a higher chemical barrier.)