True, enzymes cannot change the ∆G. However, there are many cases where an increased binding strength and rate of reactions using the products of the original r

True, enzymes cannot change the ∆G. However, there are many cases where an increased binding strength and rate of reactions using the products of the original reaction allow for a shift in equilibrium. Though, it may possibly make the system less profitable. I'm thinking of it from a biochemical perspective more so than a physical one, so take what I have written with a grain of salt. (For examples, you could look into the unprofitable steps of Glycolysis, Glyceraldehyde 3 Phosphate is not spontaneously used on its own, but the ATP used by the reaction ahead of it provides the impulse for the reaction before it. So long as the pathway is productive, they'll survive. (I enjoyed responding to this too much, thanks for the comment, mate))