Boosting the Reactivity of a Fungus-Derived Enzyme Duo

Jim Crocker
12th March, 2024

Boosting the Reactivity of a Fungus-Derived Enzyme Duo

Key Findings

  • Scientists at Van Yuzuncu Yil University developed a method to create bioplastics from biomass
  • They used a new enzyme to convert a key molecule, HMF, into a plastic precursor, FDCA
  • Combining two enzymes allowed nearly complete conversion of HMF to FDCA in 24 hours
In the quest for sustainable materials, scientists have been exploring ways to create plastics from renewable resources. One of the most promising materials in this field is 2,5-furandicarboxylic acid (FDCA), a potential replacement for petroleum-derived plastics. FDCA can be used to produce polyethylene furanoate (PEF), which is similar to the widely used polyethylene terephthalate (PET) but has a greener footprint. The challenge, however, lies in efficiently converting biomass-derived compounds into FDCA. A recent study from Van Yuzuncu Yil University[1] has made significant strides in this area. Researchers have focused on an enzyme called glyoxal oxidase (GLOX), which can transform certain aldehyde compounds into carboxylic acids. These acids are crucial intermediates in the production of FDCA. The enzyme of interest in the study, from the fungus Trametes versicolor, known as TvGLOX, was successfully produced in large amounts using the yeast Pichia pastoris. TvGLOX has shown the ability to oxidize a compound called 5-hydroxymethylfurfural (HMF) into other intermediates. HMF is a key molecule derived from biomass that can be transformed into FDCA. The process involves multiple steps, converting HMF to 2,5-diformylfuran (DFF) and then to 5-formyl-2-furancarboxylic acid (FFCA). However, TvGLOX alone couldn't complete the conversion to FDCA because it barely acted on alcohol groups present in some intermediates like HMFCA. One of the hurdles with using GLOX enzymes, including TvGLOX, is that they become inactivated over time. To address this, the researchers tested various redox activators that could rejuvenate the enzyme. They found that a combination of horseradish peroxidase and a compound called ABTS reactivated TvGLOX most effectively. By integrating TvGLOX with another enzyme, an aryl-alcohol oxidase (AAO) from Moesziomyces antarcticus (MaAAO), they achieved nearly complete conversion of HMF to FDCA in 24 hours. This two-enzyme system is particularly exciting because MaAAO was previously shown to be a robust biocatalyst, capable of accepting a wide range of substrates and withstanding harsh conditions[2]. The findings from Van Yuzuncu Yil University build on earlier research that has explored different methods and enzymes for converting HMF to FDCA. For example, studies have reported the use of galactose oxidase and lipase-mediated reactions to produce FDCA in various solvents[3], and the discovery of a bacterial aryl alcohol oxidase with improved efficiency after mutagenesis[4]. The current study expands on these earlier works by combining the strengths of different enzymes to achieve a more efficient conversion process. The significance of this research lies in its potential impact on the production of bioplastics. By finding more efficient ways to produce FDCA from renewable resources, the study contributes to the development of sustainable materials that can reduce our reliance on fossil fuels. The ability to express TvGLOX at high levels and reactivate it during the reaction process offers a scalable and potentially cost-effective approach to FDCA synthesis. In summary, the study from Van Yuzuncu Yil University represents a step forward in the biocatalytic production of FDCA. By harnessing the power of enzymes to catalyze the conversion of biomass-derived compounds, scientists are paving the way for a future where plastics are not only versatile and durable but also environmentally friendly. This research not only demonstrates a successful method for producing FDCA but also exemplifies the potential of collaborative enzyme systems in industrial biotechnology.



Main Study

1) Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade.

Published 11th March, 2024

Related Studies

2) Characterization of a thermotolerant aryl-alcohol oxidase from Moesziomyces antarcticus oxidizing 5-hydroxymethyl-2-furancarboxylic acid.

3) Enzymatic Cascade for the Synthesis of 2,5-Furandicarboxylic Acid in Biphasic and Microaqueous Conditions: 'Media-Agnostic' Biocatalysts for Biorefineries.

4) Oxidation of 5-hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601.

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