A groundbreaking study published in Microbial Biotechnology has revealed how researchers at Tokyo University of Science successfully redesigned a previously elusive bacterial enzyme into an efficient and environmentally friendly catalyst, opening new possibilities for sustainable chemical manufacturing and industrial biotechnology.
Key Highlights:
- Researchers redesign bacterial enzyme CYP107J1 into a powerful green catalyst
- Study published in Microbial Biotechnology journal
- Engineered enzyme operates without natural redox partner proteins
- Modified enzyme delivers 28-fold higher catalytic activity
- New approach could transform pharmaceutical and dye manufacturing
- Scientists successfully produced indigo dye using the engineered enzyme
- Breakthrough offers a low-cost pathway for sustainable industrial oxidation processes
The research provides significant insights into enzyme engineering by transforming the cytochrome P450 enzyme CYP107J1, derived from Bacillus subtilis, into a hydrogen peroxide-driven peroxygenase capable of functioning independently of natural redox partner proteins.
Breakthrough in Bacterial Enzyme Engineering
Industrial oxidation chemistry plays a vital role in modern manufacturing, accounting for nearly one-third of all industrial chemical processes worldwide. However, conventional oxidation methods often require high temperatures, high pressures, and hazardous oxidising agents.
Scientists have increasingly turned to cytochrome P450 monooxygenases, a family of naturally occurring enzymes known for carrying out highly selective oxidation reactions under mild conditions.
Despite Bacillus subtilis being one of the most extensively studied bacterial species, one of its eight P450 enzymes, CYP107J1, remained largely uncharacterised because researchers could not identify its natural redox partner proteins required for activation.
To overcome this challenge, a research team led by Professor Toshiki Furuya of Tokyo University of Science developed a strategy that completely bypasses the need for redox partner proteins.
The findings were published in Volume 19, Issue 5 of Microbial Biotechnology on May 4, 2026.
Engineered Enzyme Delivers Superior Performance
The team initially confirmed that CYP107J1 could oxidise 4-alkylbenzoic acids when paired with substitute redox partners in Escherichia coli cells.
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However, the enzyme’s activity remained relatively weak.
Researchers then introduced two precisely targeted amino acid modifications within the enzyme’s active site, transforming it into a hydrogen peroxide-driven peroxygenase.
Structural modelling confirmed that the selected mutations were appropriately positioned to enhance catalytic performance.
The result was a dramatic increase in efficiency.
According to the study, the engineered bacterial enzyme demonstrated a 28-fold improvement in catalytic activity toward 4-hexylbenzoic acid compared to the original enzyme while maintaining its selectivity.
Potential Applications in Pharmaceuticals and Dye Production
One of the most surprising discoveries was the enzyme’s ability to convert indole into indigo, a commercially valuable blue dye widely used in textile manufacturing.
By combining only the enzyme, substrate, and hydrogen peroxide, researchers successfully produced indigo at rates exceeding those reported for previously studied P450 peroxygenases.
Professor Furuya said the simplified reaction mechanism offers important advantages for both enzyme research and industrial applications.
“The method used in this study simplified the driving mechanism of the P450 reaction itself, making it effective not only for analysing enzymes with unknown functions but also for applying them as catalysts for synthesising useful compounds,” he explained.
Implications for Sustainable Manufacturing
The researchers believe the two-mutation engineering strategy could serve as a practical blueprint for unlocking the potential of many other poorly understood P450 enzymes without first identifying their natural redox partners.
Such advances could significantly expand the industrial use of engineered enzymes in the production of pharmaceuticals, specialty chemicals, dyes, and other high-value products.
By reducing reliance on harsh industrial oxidation processes, the innovation could contribute to more sustainable manufacturing practices while lowering energy consumption and environmental impact.
Future Research
The team is currently working to further enhance the catalytic efficiency of the modified CYP107J1 enzyme.
Professor Furuya noted that enzymes belonging to the CYP107J subfamily are widely distributed among Bacillus species, suggesting considerable untapped potential for future industrial applications.
“The findings from this study will facilitate further exploitation of their catalytic potential,” he said.
The research was conducted by Tokyo University of Science in collaboration with Dr. Stephen Bell and his team at the University of Adelaide.
Study Details
Title: Characterization of the Orphan Cytochrome P450 CYP107J1 From Bacillus subtilis Through Peroxygenase Activity Engineering
Journal: Microbial Biotechnology
DOI: 10.1111/1751-7915.70369
