The most credible “quantum lever” in fermentation is not macroscopic entanglement across cells; it is the possibility that some rate‑limiting metabolic steps already rely partly on quantum tunneling of hydrogen, and that enzymes modulate tunneling through protein dynamics and active-site geometry. This implies a nontrivial proposition: for specific steps, improving yield may require engineering not only binding and classical transition-state stabilization, but also the barrier width and donor–acceptor distance distribution that controls tunneling probability. Reviews linking hydrogen tunneling to protein dynamics make precisely this point: a successful treatment of H‑tunneling requires multidimensional models that include environmental/protein motions, rather than a purely static barrier picture.

The constraint is equally important:even if tunneling enhances a specific enzyme step, fermentation yield is a systems property, and local kinetic gains will translate into yield only when pathway control structure and cellular constraints permit that gain to propagate to net production.

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