4.6 Article

Sustainable Approach for Peroxygenase-Catalyzed Oxidation Reactions Using Hydrogen Peroxide Generated from Spent Coffee Grounds and Tea Leaf Residues

Journal

ACS OMEGA
Volume 7, Issue 23, Pages 20259-20266

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acsomega.2c02186

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Peroxygenases are promising catalysts for chemical oxidation, but the current production of hydrogen peroxide (H2O2) requires significant energy input and generates waste. This study successfully utilized waste coffee grounds and tea leaf residues to produce H2O2, which was then used in peroxygenase-catalyzed oxidation reactions. This provides a simple, cost-effective, and sustainable method for synthesizing valuable chemicals.
Peroxygenases are promising catalysts for use in the oxidation of chemicals as they catalyze the direct oxidation of a variety of compounds under ambient conditions using hydrogen peroxide (H2O2) as an oxidant Although the use of peroxygenases provides a simple method for oxidation of chemicals, the anthraquinone process currently used to produce H2O2 requires significant energy input and generates considerable waste, which negatively affects process sustainability and production costs. Thus, generating H2O2 for peroxygenases on site using an environmentally benign method would be advantageous. Here, we utilized spent coffee grounds (SCGs) and tea leaf residues (TLRs) for the production of H2O2 . These waste biomass products reacted with molecular oxygen and effectively generated H(2)O(2 )in sodium phosphate buffer. The resulting H2O2 was utilized by the bacterial P450 peroxygenase, CYP152A1. Both SCG-derived and TLR-derived H2O2 promoted the CYP152A1-catalyzed oxidation of 4-methoxy-1-naphthol to Russig's blue as a model reaction. In addition, when CYP152A1 was incubated with styrene, the SCG and TLR solutions enabled the synthesis of styrene oxide and phenylacetaldehyde. This new approach using waste biomass provides a simple, costeffective, and sustainable oxidation method that should be readily applicable to other peroxygenases for the synthesis of a variety of valuable chemicals.

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