Akademik Veri Yönetim Sistemi
VI. International Enzyme and Bioprocess Days, Kocaeli, Türkiye, 27 - 29 Ağustos 2025, ss.36-37, (Özet Bildiri)
Glyoxal oxidases are copper radical enzymes that catalyze the oxidation of aldehydes to carboxylic acids
while simultaneously reducing molecular oxygen to hydrogen peroxide. These enzymes exhibit notable
activity on furan-based substrates such as 5-hydroxymethylfurfural (HMF), making them promising
biocatalysts for the sustainable production of 2,5-furandicarboxylic acid (FDCA), a key precursor for
bioplastics. In this study, we report the heterologous expression of a novel glyoxal oxidase from Trametes
versicolor (TvGLOX) in Pichia pastoris (currently reclassified as Komagataella phaffii), followed by its
detailed biochemical characterization. TvGLOX showed efficient oxidation of several aldehyde substrates,
including glyoxylic acid, methyl glyoxal, HMF, 2,5-diformylfuran (DFF), and 5-formyl-2-furancarboxylic
acid (FFCA). However, the enzyme exhibited limited activity toward alcohol groups, such as those in 5-
hydroxymethyl-2-furancarboxylic acid (HMFCA), which restricts direct FDCA formation from HMF. To
overcome enzyme inactivation and improve catalytic efficiency, a two-enzyme system was developed by
coupling TvGLOX with recombinant Moesziomyces antarcticus aryl-alcohol oxidase (MaAAO). This
system enabled near-complete conversion of 8 mM HMF to FDCA within 24 hours, demonstrating effective
substrate turnover and enzyme reactivation. Our findings highlight a robust enzymatic approach for green
and sustainable bioplastic precursor synthesis, contributing to the advancement of environmentally friendly
chemical manufacturing.