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Researchers have characterized PsGalOx, the first galactose oxidase reported from bacteria. The enzyme uses molecular oxygen to oxidize sugars and alcohols under mild biological conditions. Laboratory engineering increased measured efficiency by 40- to 1,800-fold across different test substrates, but that range does not mean a universal improvement and does not yet show that PsGalOx can run a commercial pharmaceutical or food process.
The work, led by Instituto de Tecnologia Química e Biológica António Xavier (ITQB NOVA) at NOVA University Lisbon, was published in Chem & Bio Engineering on October 11, 2026 (DOI: 10.1021/cbe.6c00167).
What the team discovered
Galactose oxidases convert primary alcohol groups in sugars and related molecules into oxidized products while reducing molecular oxygen. Enzymes can perform this chemistry in water and at comparatively mild temperatures and pH, whereas conventional oxidation may require harsher stoichiometric oxidants, elevated temperatures and generate more problematic waste.
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Before this study, the best-characterized galactose oxidases were fungal. PsGalOx expands the family with a bacterial scaffold that can be produced and engineered in bacterial systems. That matters because a new evolutionary starting point may offer different substrate preferences, stability characteristics and manufacturing options than familiar fungal enzymes.
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“For several years, the enzyme proved exceptionally difficult to produce in a soluble form and therefore to characterize,” said Lígia Martins, who leads the ITQB NOVA Microbial & Enzyme Technology laboratory.
How PsGalOx is built
A catalytic module plus two binding modules
PsGalOx has a catalytic module and two nearly identical carbohydrate-binding modules. The duplicated modules share approximately 80% sequence identity, yet they do different jobs. One primarily improves binding to sugars; the other mainly supports the protein’s structural stability. Tomás Frazão, the study’s first author and an ITQB NOVA doctoral student, described them as modules that “have evolved distinct functions.”
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Why the architecture was difficult to express
The unusual modular arrangement helped explain why early production in bacterial cells yielded little soluble enzyme. AlphaFold structural predictions gave the researchers a model of the protein’s shape and indicated where changes might relieve the production problem. As Martins put it, AlphaFold’s predictions were a turning point because they helped identify substitutions that could improve expression.
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Directed evolution improved soluble production
The team combined computationally guided changes with directed evolution. They introduced mutations, screened thousands of bacterial colonies and recombined binding modules to make hybrid versions. The resulting variants produced more soluble PsGalOx, giving the researchers enough usable enzyme for clearer biochemical measurements.
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Separating expression from catalytic improvement
An important result is methodological as well as numerical: an increase in activity measured from a culture does not automatically mean that each enzyme molecule performs chemistry faster. In the early rounds, much of the gain came from host cells making more soluble protein. By separating total soluble expression from intrinsic catalytic performance, the researchers could direct later rounds toward the property that actually needed improvement.
What “40 to 1,800 times more efficient” means
The reported 40- to 1,800-fold range compares engineered variants with the starting enzyme across different sugars and alcohols in laboratory tests. It is not one universal factor for PsGalOx, and it does not establish performance in a production reactor. The value depends on the substrate and the measurement used in each experiment.
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Why an oxygen-driven enzyme could enable greener chemistry
Oxidized sugars and alcohols are useful intermediates. Depending on the molecule and the downstream process, they can feed routes to pharmaceutical active ingredients, food ingredients, flavors, fragrances and materials. Replacing a harsh chemical oxidant with oxygen and a reusable biocatalyst could reduce hazardous reagent use and simplify waste handling.
That benefit is a process hypothesis, not a demonstrated commercial outcome for PsGalOx. The study establishes a promising enzyme platform and laboratory engineering results; it does not report a completed drug or food-ingredient manufacturing route using the enzyme.
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PsGalOx compared with other oxidation options
| Comparison axis | PsGalOx platform | Conventional chemical oxidation | Fungal galactose oxidases |
|---|---|---|---|
| Oxidant | Molecular oxygen in an enzymatic reaction | Often harsher stoichiometric oxidants | Typically oxygen-driven enzymatic oxidation |
| Operating environment | Mild biological conditions demonstrated in laboratory work | May require higher temperatures, stronger reagents or less benign solvents | Biological conditions, with requirements varying by enzyme |
| Expression angle | Bacterial scaffold engineered for higher soluble production | Not applicable to enzyme expression | Different host and protein-production challenges |
| Substrate evidence | Different sugars and alcohols tested; practical manufacturing substrates remain a target | Depends on the particular chemical route | Established family, but substrate scope varies by enzyme and engineering |
| Scale-up evidence for this platform | No industrial reactor, process-economics or commercial-product data reported | Industrial data depend on the selected process | Varies by enzyme and process |
Can PsGalOx make greener drugs or food ingredients now?
Not yet. The current evidence supports PsGalOx as a laboratory platform, not as a validated manufacturing catalyst. The researchers say they plan to continue engineering it toward substrates of practical interest. A useful production process would still need to demonstrate, at minimum:
- Reliable conversion of a named pharmaceutical, food, fragrance or materials precursor at useful concentration.
- High selectivity and yield in the presence of real feedstocks and product mixtures.
- Operational stability over the reaction time required by a plant-scale process.
- Efficient enzyme manufacture, recovery or reuse and acceptable oxygen-transfer performance.
- Purification, waste, energy and cost advantages over the incumbent chemical route.
- Reproducibility beyond colony screens and small-scale laboratory assays.
None of those industrial validation measures is reported for PsGalOx in the available study or institutional account. The phrase “greener drug and food ingredient production” therefore describes the direction this work could support, not a process already replacing commercial chemistry.
How this fits earlier enzyme-engineering work
PsGalOx is not the first bacterial carbohydrate oxidase studied. A 2022 study of NagOx, a different enzyme from Ralstonia solanacearum, showed that engineering could change acceptance of monosaccharides and disaccharides. A 2024 study reported stable, promiscuous engineered galactose oxidases with expanded activity. Those results provide precedent for directed evolution and computational design, but they are not performance data for PsGalOx.
The new bacterial scaffold gives researchers another system in which to study how binding and stability evolve. Martins said the team wants to use it to understand specificity and identify robust, versatile scaffolds for new biocatalysts.
What to watch next
The decisive next results will be substrate-specific demonstrations rather than another headline fold-change: conversion of a named practical intermediate, reaction performance at useful concentration, stability during extended operation and a comparison with the existing chemical route. Until those data appear, PsGalOx is best understood as an engineered starting point with unusually strong laboratory gains and substantial scale-up work ahead.
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