Carbonic Anhydrase Enhanced UV-Crosslinked PEG-DA/PEO Extruded Hydrogel Flexible Filaments and Durable Grids for CO2 Capture

Shen, Jialong; Zhang, Sen; Fang, Xiaomeng; Salmon, Sonja

doi:10.3390/gels9040341

Cited by 8 publications

(3 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some CA mutants can accelerate proton transfer, the rate-limiting step for CA turnover [96]. Another reason for increasing CA activity is the urgent need for the green ways of industrial CO 2 sequestration [106], which we mentioned above.…”

Section: Ca I Ca Ii and Ca Ii-t200h (Also Four-state Enzymes)mentioning

confidence: 99%

Theoretical Improvements in Enzyme Efficiency Associated with Noisy Rate Constants and Increased Dissipation

Juretić,

Bonačić Lošić

2024

Entropy

View full text Add to dashboard Cite

Previous studies have revealed the extraordinarily large catalytic efficiency of some enzymes. High catalytic proficiency is an essential accomplishment of biological evolution. Natural selection led to the increased turnover number, kcat, and enzyme efficiency, kcat/KM, of uni–uni enzymes, which convert a single substrate into a single product. We added or multiplied random noise with chosen rate constants to explore the correlation between dissipation and catalytic efficiency for ten enzymes: beta-galactosidase, glucose isomerase, β-lactamases from three bacterial strains, ketosteroid isomerase, triosephosphate isomerase, and carbonic anhydrase I, II, and T200H. Our results highlight the role of biological evolution in accelerating thermodynamic evolution. The catalytic performance of these enzymes is proportional to overall entropy production—the main parameter from irreversible thermodynamics. That parameter is also proportional to the evolutionary distance of β-lactamases PC1, RTEM, and Lac-1 when natural or artificial evolution produces the optimal or maximal possible catalytic efficiency. De novo enzyme design and attempts to speed up the rate-limiting catalytic steps may profit from the described connection between kinetics and thermodynamics.

show abstract

Section: Ca I Ca Ii and Ca Ii-t200h (Also Four-state Enzymes)mentioning

confidence: 99%

Theoretical Improvements in Enzyme Efficiency Associated with Noisy Rate Constants and Increased Dissipation

Juretić,

Bonačić Lošić

2024

Entropy

View full text Add to dashboard Cite

show abstract

“…Compared to post-immobilization approaches, incorporation immobilization can achieve high mass fractions of enzymes using simple procedures [ 110 ]. In this strategy, enzyme immobilization occurs simultaneously during support material formation [ 213 ]. Thus, either a mild fiber fabrication procedure or a robust enzyme is required, which restricts the selection of raw materials.…”

Section: Fibrous Membrane Immobilization Supportsmentioning

confidence: 99%

Developing Enzyme Immobilization with Fibrous Membranes: Longevity and Characterization Considerations

2023

Self Cite

View full text Add to dashboard Cite

Fibrous membranes offer broad opportunities to deploy immobilized enzymes in new reactor and application designs, including multiphase continuous flow-through reactions. Enzyme immobilization is a technology strategy that simplifies the separation of otherwise soluble catalytic proteins from liquid reaction media and imparts stabilization and performance enhancement. Flexible immobilization matrices made from fibers have versatile physical attributes, such as high surface area, light weight, and controllable porosity, which give them membrane-like characteristics, while simultaneously providing good mechanical properties for creating functional filters, sensors, scaffolds, and other interface-active biocatalytic materials. This review examines immobilization strategies for enzymes on fibrous membrane-like polymeric supports involving all three fundamental mechanisms of post-immobilization, incorporation, and coating. Post-immobilization offers an infinite selection of matrix materials, but may encounter loading and durability issues, while incorporation offers longevity but has more limited material options and may present mass transfer obstacles. Coating techniques on fibrous materials at different geometric scales are a growing trend in making membranes that integrate biocatalytic functionality with versatile physical supports. Biocatalytic performance parameters and characterization techniques for immobilized enzymes are described, including several emerging techniques of special relevance for fibrous immobilized enzymes. Diverse application examples from the literature, focusing on fibrous matrices, are summarized, and biocatalyst longevity is emphasized as a critical performance parameter that needs increased attention to advance concepts from lab scale to broader utilization. This consolidation of fabrication, performance measurement, and characterization techniques, with guiding examples highlighted, is intended to inspire future innovations in enzyme immobilization with fibrous membranes and expand their uses in novel reactors and processes.

show abstract

“…Some CA mutants can accelerate the proton transfer, the rate-limiting step for CA turnover [94]. Another reason for increasing CA activity is the urgent need for green ways of industrial CO2 sequestration [104] we mentioned above.…”

Section: Ca I Caii Caii-t200h Chapter (Also 4-state Enzymes)mentioning

confidence: 99%

Computational Improvements of Enzyme Efficiency k<sub>cat</sub>/K<sub>M</sub> by Increasing Noise and Dissipation

Juretić,

Bonačić Lošić

2023

Preprint

View full text Add to dashboard Cite

Wolfenden and his coworkers observed the astronomical numbers for the catalytic proficiency of some enzymes. We connected that pinnacle of biological evolution to the universal thermodynamic evolution. We added or multiplied a random noise with chosen rate constants to explore the correlation between dissipation and enzyme efficiency for ten enzymes: beta-galactosidase, glucose isomerase, β-lactamases from three bacterial strains, ketosteroid isomerase, triosephosphate isomerase, and carbonic anhydrase I, II, and T200H. The turnover number kcat and catalytic efficiency kcat/KM are proportional to the overall entropy production – the main parameter from irreversible thermodynamics. For most enzymes with the Michaelis-Menten type cycle kinetics, the best increase in the forward kcat/KM follows after increasing the equilibrium constant of substrate-enzyme association. The Discussion section emphasizes the role of biological evolution in harvesting order (high enzyme efficiency) from disorder (high noise and dissipation). It also connects the applications of the maximum partial entropy production theorem in optimizing enzyme kinetics (D. Juretić "Bioenergetics - A Bridge across Life and Universe") with the present total entropy production role analysis. De novo enzyme design and various attempts to speed up the rate-limiting catalytic steps may profit from our theoretical insights.

show abstract

Carbonic Anhydrase Enhanced UV-Crosslinked PEG-DA/PEO Extruded Hydrogel Flexible Filaments and Durable Grids for CO2 Capture

Cited by 8 publications

References 52 publications

Theoretical Improvements in Enzyme Efficiency Associated with Noisy Rate Constants and Increased Dissipation

Theoretical Improvements in Enzyme Efficiency Associated with Noisy Rate Constants and Increased Dissipation

Developing Enzyme Immobilization with Fibrous Membranes: Longevity and Characterization Considerations

Computational Improvements of Enzyme Efficiency k<sub>cat</sub>/K<sub>M</sub> by Increasing Noise and Dissipation

Contact Info

Product

Resources

About