scholarly journals Multi-enzyme cascade reactions using protein–polymer surfactant self-standing films

2017 ◽  
Vol 53 (13) ◽  
pp. 2094-2097 ◽  
Author(s):  
Thomas Farrugia ◽  
Adam W. Perriman ◽  
Kamendra P. Sharma ◽  
Stephen Mann
Keyword(s):  
Cascade Reactions ◽  
Hierarchical Assembly ◽  
Protein Polymer ◽  
Enzyme Cascade ◽  
Catalytically Active ◽  
Polymer Surfactant

Self-supporting bio-catalytically active multi-enzyme films fabricated via hierarchical assembly of enzyme–polymer surfactant nanoconjugates are capable of sustaining cascade reactions.

scholarly journals Microfluidics Featuring Multilayered Hydrogel Assemblies Enable Real-Time NMR-Monitoring of Enzyme Cascade Reactions

2020 ◽  
Author(s):  
Nurdiana Nordin ◽  
lorenzo bordonali ◽  
Hossein Davoodi ◽  
Novindi Dwi Ratnawati ◽  
Gudrun Gygli ◽  
...  
Keyword(s):  
Real Time ◽  
Functional Performance ◽  
Cascade Reactions ◽  
Inhibitory Effect ◽  
Resonance Spectroscopy ◽  
Reaction Cell ◽  
Enzyme Cascade ◽  
Sensing Applications ◽  
Progress Curve ◽  
Michaelis Constants

Compartmentalized chemical reactions at the microscale are interesting from many perspectives including (multi)functional surfaces and biotechnology. Monitoring the molecular content as a measure of functional performance at these small scales is challenging. As a means to address this challenge, we leverage microtechnology and biocompatible materials to integrate a compact, reconfigurable reaction cell featuring electrochemical functionality with high-resolution nuclear magnetic resonance spectroscopy (NMR). We demonstrate the operation of this system by monitoring the activity of enzymes immobilized in chemically distinct layers within a multi-layered chitosan hydrogel assembly. As a benchmark, we observed the parallel activities of urease (Urs), catalase (Cat), and glucose oxidase (GOx) by recording NMR spectra to extract reagent and product concentrations in real-time. As a result, simultaneous monitoring of a cooperative enzymatic process (GOx + Cat) together with an independent process (Urs) is achieved. Using Michaelis-Menten progress curve analysis of the NMR data, kinetic data is extracted: in the case of GOx, the Michaelis constants (K<sub>M</sub>) are consistent with previous reports, while for Urs, deviations are observed, attributed to an inhibitory effect under our reaction conditions. The system therefore enables the construction of complex reaction cascades with spatial control, as would be interesting in, for example, metabolic engineering and multiplexed sensing applications.

Multi‐enzyme Cascade Reactions in Metal‐organic Frameworks

2020 ◽  
Vol 20 (10) ◽  
pp. 1100-1116 ◽  
Author(s):  
Jieying Liang ◽  
Kang Liang
Keyword(s):  
Metal Organic Frameworks ◽  
Cascade Reactions ◽  
Enzyme Cascade ◽  
Metal Organic

scholarly journals Recent Advances in Enzymatic and Chemoenzymatic Cascade Processes

Catalysts ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1258
Author(s):  
Noelia Losada-Garcia ◽  
Zaida Cabrera ◽  
Paulina Urrutia ◽  
Carla Garcia-Sanz ◽  
Alicia Andreu ◽  
...  
Keyword(s):  
Organic Chemistry ◽  
Solid Phase ◽  
Cascade Reactions ◽  
Review Article ◽  
The Novel ◽  
Enzyme Cascade ◽  
Cascade Processes ◽  
Novel Strategy ◽  
Substantial Interest

Cascade reactions have been described as efficient and universal tools, and are of substantial interest in synthetic organic chemistry. This review article provides an overview of the novel and recent achievements in enzyme cascade processes catalyzed by multi-enzymatic or chemoenzymatic systems. The examples here selected collect the advances related to the application of the sequential use of enzymes in natural or genetically modified combination; second, the important combination of enzymes and metal complex systems, and finally we described the application of biocatalytic biohybrid systems on in situ catalytic solid-phase as a novel strategy. Examples of efficient and interesting enzymatic catalytic cascade processes in organic chemistry, in the production of important industrial products, such as the designing of novel biosensors or bio-chemocatalytic systems for medicinal chemistry application, are discussed

Enzyme cascade reactions: synthesis of furandicarboxylic acid (FDCA) and carboxylic acids using oxidases in tandem

2015 ◽  
Vol 17 (6) ◽  
pp. 3271-3275 ◽  
Author(s):  
Shane M. McKenna ◽  
Silke Leimkühler ◽  
Susanne Herter ◽  
Nicholas J. Turner ◽  
Andrew J. Carnell
Keyword(s):  
Carboxylic Acids ◽  
Cascade Reactions ◽  
Preparative Scale ◽  
Mild Conditions ◽  
Enzyme Cascade ◽  
Furandicarboxylic Acid

Three enzymes are combined under mild conditions for the preparative scale oxidation of HMF to FDCA and a range of 10 alcohols.

Fusion proteins of an enoate reductase and a Baeyer-Villiger monooxygenase facilitate the synthesis of chiral lactones

2017 ◽  
Vol 398 (1) ◽  
pp. 31-37 ◽  
Author(s):  
Christin Peters ◽  
Florian Rudroff ◽  
Marko D. Mihovilovic ◽  
Uwe T. Bornscheuer
Keyword(s):  
Fusion Protein ◽  
Fusion Proteins ◽  
Reaction Rates ◽  
Cascade Reactions ◽  
Product Formation ◽  
Similar Reaction ◽  
Enzyme Cascade ◽  
Enoate Reductase ◽  
Chiral Lactones

Abstract Nature uses the advantages of fusion proteins for multi-step reactions to facilitate the metabolism in cells as the conversion of substrates through intermediates to the final product can take place more rapidly and with less side-product formation. In a similar fashion, also for enzyme cascade reactions, the fusion of biocatalysts involved can be advantageous. In the present study, we investigated fusion of an alcohol dehydrogenase (ADH), an enoate reductase (ERED) and a Baeyer-Villiger monooxygenase (BVMO) to enable the synthesis of (chiral) lactones starting from unsaturated alcohols as substrates. The domain order and various linkers were studied to find optimal conditions with respect to expression levels and enzymatic activities. Best results were achieved for the ERED xenobiotic reductase B (XenB) from Pseudomonas putida and the cyclohexanone monooxygenase (CHMO) from Acinetobacter sp., whereas none of the ADHs studied could be fused successfully. This fusion protein together with separately supplied ADH resulted in similar reaction rates in in vivo biocatalysis reactions. After 1.5 h we could detect 40% more dihydrocarvone lactone in in vivo reactions with the fusion protein and ADH then with the single enzymes.

scholarly journals Tetrahymena Telomerase Protein p65 Induces Conformational Changes throughout Telomerase RNA (TER) and Rescues Telomerase Reverse Transcriptase and TER Assembly Mutants

2010 ◽  
Vol 30 (20) ◽  
pp. 4965-4976 ◽  
Author(s):  
Andrea J. Berman ◽  
Anne R. Gooding ◽  
Thomas R. Cech
Keyword(s):  
Reverse Transcriptase ◽  
Single Molecule ◽  
Conformational Changes ◽  
Mutational Analysis ◽  
Telomerase Activity ◽  
Telomerase Reverse Transcriptase ◽  
Telomerase Rna ◽  
Hierarchical Assembly ◽  
Family Protein ◽  
Catalytically Active

ABSTRACT The biogenesis of the Tetrahymena telomerase ribonucleoprotein particle (RNP) is enhanced by p65, a La family protein. Single-molecule and biochemical studies have uncovered a hierarchical assembly of the RNP, wherein the binding of p65 to stems I and IV of telomerase RNA (TER) causes a conformational change that facilitates the subsequent binding of telomerase reverse transcriptase (TERT) to TER. We used purified p65 and variants of TERT and TER to investigate the conformational rearrangements that occur during RNP assembly. Nuclease protection assays and mutational analysis revealed that p65 interacts with and stimulates conformational changes in regions of TER beyond stem IV. Several TER mutants exhibited telomerase activity only in the presence of p65, revealing the importance of p65 in promoting the correct RNP assembly pathway. In addition, p65 rescued TERT assembly mutants but not TERT activity mutants. Taken together, these results suggest that p65 stimulates telomerase assembly and activity in two ways. First, by sequestering stems I and IV, p65 limits the ensemble of structural conformations of TER, thereby presenting TERT with the active conformation of TER. Second, p65 acts as a molecular buttress within the assembled RNP, mutually stabilizing TER and TERT in catalytically active conformations.

scholarly journals Encapsulated Hydrogels by E-beam Lithography and Their Use in Enzyme Cascade Reactions

Langmuir ◽  
2016 ◽  
Vol 32 (16) ◽  
pp. 4043-4051 ◽  
Author(s):  
Rock J. Mancini ◽  
Samantha J. Paluck ◽  
Erhan Bat ◽  
Heather D. Maynard
Keyword(s):  
Cascade Reactions ◽  
Enzyme Cascade
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