ArticleBiotechnology and bioengineering2019
Stabilization of cyclohexanone monooxygenase by computational and experimental library design.
Article in Biotechnology and bioengineering, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 39 citations in OpenAlex.
- Recombinant Expression and Characterization of a Novel Type I Baeyer-Villiger Monooxygenase from aInternational journal of molecular sciences · 2025Article
- Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification.Nature communications · 2024Article
- ALDELE: All-Purpose Deep Learning Toolkits for Predicting the Biocatalytic Activities of Enzymes.Journal of chemical information and modeling · 2024Article
- Increased Thermostability of an Engineered Flavin-Containing Monooxygenase to Remediate Trimethylamine in Fish Protein Hydrolysates.Applied and environmental microbiology · 2023Article
- Structure- and computational-aided engineering of an oxidase to produce isoeugenol from a lignin-derived compound.Nature communications · 2022Article
- Mutations Increasing Cofactor Affinity, Improve Stability and Activity of a Baeyer-Villiger Monooxygenase.ACS catalysis · 2022Article
- Article
- Investigation of a New Type I Baeyer-Villiger Monooxygenase from Amycolatopsis thermoflava Revealed High Thermodynamic but Limited Kinetic Stability.Chembiochem : a European journal of chemical biology · 2020Article
- Article
- Robust ω-Transaminases by Computational Stabilization of the Subunit Interface.ACS catalysis · 2020Article
- Structure-Based Redesign of a Self-Sufficient Flavin-Containing Monooxygenase towards Indigo Production.International journal of molecular sciences · 2019Article
- Stabilization of cyclohexanone monooxygenase by computational and experimental library design.Biotechnology and bioengineering · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes often by far exceed the activity, selectivity, and sustainability achieved with chemical catalysts. One of the main reasons for the lack of biocatalysis in the chemical industry is the poor stability exhibited by many enzymes when exposed to process conditions. This dilemma is exemplified in the usually very temperature-sensitive enzymes catalyzing the Baeyer-Villiger reaction, which display excellent stereo- and regioselectivity and offer a green alternative to the commonly used, explosive peracids. Here we describe a protein engineering approach applied to cyclohexanone monooxygenase from Rhodococcus sp. HI-31, a substrate-promiscuous enzyme that efficiently catalyzes the production of the nylon-6 precursor ε-caprolactone. We used a framework for rapid enzyme stabilization by computational libraries (FRESCO), which predicts protein-stabilizing mutations. From 128 screened point mutants, approximately half had a stabilizing effect, albeit mostly to a small degree. To overcome incompatibility effects observed upon combining the best hits, an easy shuffled library design strategy was devised. The most stable and highly active mutant displayed an increase in unfolding temperature of 13°C and an approximately 33x increase in half-life at 30°C. In contrast to the wild-type enzyme, this thermostable 8x mutant is an attractive biocatalyst for biotechnological applications.
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