ArticleACS sustainable chemistry & engineering2024
Stability Increase of Phenolic Acid Decarboxylase by a Combination of Protein and Solvent Engineering Unlocks Applications at Elevated Temperatures.
Article in ACS sustainable chemistry & engineering, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Engineering the substrate scope of the thermostable phenolic acid decarboxylase N31 towards sterically hindered phenolic acids.Protein science : a publication of the Protein Society · 2026Article
- Scaling Up Is Not the Same but Bigger: Overcoming (Some) Limitations in Enzymatic Decarboxylations in Rotating Bed Reactors in Deep Eutectic Solvents.Organic process research & development · 2026Article
- Ancestral Protein Reconstruction Uncovers a Thermotolerant Rieske Oxygenase with EnhancedACS synthetic biology · 2026Article
- Screening of a 4-Ethylguaiacol-ProducingMicroorganisms · 2026Article
- Molar-Scale Phenolic Acid Decarboxylation Using Thermostable Biocatalysts and Enzyme-Compatible Deep Eutectic Solvents.ChemSusChem · 2025Article
- Multiscale metabolic engineering in biological lignin valorization.Innovation (Cambridge (Mass.)) · 2025Review
- Fantastic Ferulic Acid Esterases and Their Functions.International journal of molecular sciences · 2025Review
- Biotransformation of Phenolic Acids in Foods: Pathways, Key Enzymes, and Technological Applications.Foods (Basel, Switzerland) · 2025Review
- Magnetizing Biotech-Advances in (In Vivo) Magnetic Enzyme Immobilization.Engineering in life sciences · 2025Review
- Ancestral Sequence Reconstruction for Designing Biocatalysts and Investigating their Functional Mechanisms.JACS Au · 2024Review
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
Abstract
Enzymatic decarboxylation of biobased hydroxycinnamic acids gives access to phenolic styrenes for adhesive production. Phenolic acid decarboxylases are proficient enzymes that have been applied in aqueous systems, organic solvents, biphasic systems, and deep eutectic solvents, which makes stability a key feature. Stabilization of the enzyme would increase the total turnover number and thus reduce the energy consumption and waste accumulation associated with biocatalyst production. In this study, we used ancestral sequence reconstruction to generate thermostable decarboxylases. Investigation of a set of 16 ancestors resulted in the identification of a variant with an unfolding temperature of 78.1 °C and a half-life time of 45 h at 60 °C. Crystal structures were determined for three selected ancestors. Structural attributes were calculated to fit different regression models for predicting the thermal stability of variants that have not yet been experimentally explored. The models rely on hydrophobic clusters, salt bridges, hydrogen bonds, and surface properties and can identify more stable proteins out of a pool of candidates. Further stabilization was achieved by the application of mixtures of natural deep eutectic solvents and buffers. Our approach is a straightforward option for enhancing the industrial application of the decarboxylation process.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.