A critical review of the potential of fermentation processes for production of bulk chemicals in a future circular economy.

The use of plastics in a wide range of applications has grown substantially over recent decades, resulting in enormous growth in production volumes to meet demand. Though a wide range of biomass-derived chemicals and materials are available on the market, the production volumes of such renewable alternatives are currently not sufficient to replace their fossil-based analogues due to various factors, in particular cost-effectiveness. Hence, the majority of plastics are still industrially produced from fossil-based feedstocks. Moreover, various reports have clearly raised concern about the plastics that are not recycled at their end-of-life and instead end up in landfills or the oceans. To avoid further pollution of our planet, it is highly desirable to develop recycling processes that use plastic waste as feedstock. Chemical recycling processes could potentially offer a solution, since they afford monomers from which new polymers can be produced, with the same performance as virgin plastics. In this manuscript, the opportunities for using either chemical or biochemical (i.e., enzymatic) approaches in the depolymerization of polycondensation polymers for recycling purposes are reviewed. Our aim is to highlight the strategies that have been developed so far to break down plastic waste into monomers, providing the first step in the development of chemical recycling processes for plastic waste, and to create a renewed awareness of the need to valorize plastic waste by efficiently transforming it into virgin plastics.

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A number of oxidoreductases from the VAO/para-cresol methylhydroxylase flavoprotein family catalyze the oxidation of para-substituted phenols. One of the best-studied is vanillyl-alcohol oxidase (VAO) from the fungus Penicillium simplicissimum. For oxidation of phenols by VAO to occur, they must first be bound in the active site of the enzyme in their phenolate anion form. The crystal structure of VAO reveals that two tyrosine residues, Tyr-108 and Tyr-503, are positioned to facilitate this deprotonation. To investigate their role in catalysis, we created three VAO variants, Y108F, Y503F, and Y108F/Y503F, and studied their biochemical properties. Steady-state kinetics indicated that the presence of at least one of the tyrosine residues is essential for efficient catalysis by VAO. Stopped-flow kinetics revealed that the reduction of VAO by chavicol or vanillyl alcohol occurs at two different rates: k_obs1, which corresponds to its reaction with the deprotonated form of the substrate, and k_obs2, which corresponds to its reaction with the protonated form of the substrate. In Y108F, Y503F, and Y108F/Y503F, the relative contribution of k_obs2 to the reduction is larger than in wild-type VAO, suggesting deprotonation is impaired in these variants. Binding studies disclosed that the competitive inhibitor isoeugenol is predominantly in its deprotonated form when bound to wild-type VAO, but predominantly in its protonated form when bound to the variants. These results indicate that Tyr-108 and Tyr-503 are responsible for the activation of substrates in VAO, providing new insights into the catalytic mechanism of VAO and related enzymes that oxidize para-substituted phenols.