Co-Immobilization of Ketoreductase and Glucose Dehydrogenase

Petrovičová, Tatiana; Markošová, Kristína; Hegyi, Zuzana; Smonou, Ioulia; Rosenberg, Michal; Rebroš, Martin

doi:10.3390/catal8040168

Cited by 23 publications

(32 citation statements)

References 23 publications

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“…However, the industrial applications of laccase are still seriously limited owing to their poor stability and high cost [7]. It is well known that these limitations can be overcome by immobilization technology [8][9][10][11][12]. In earlier studies, Rogalski et al immobilized laccase on controlled porosity glass and measured its activity in the aqueous solution containing organic solvents [13].…”

Section: Introductionmentioning

confidence: 99%

An Improved Method to Encapsulate Laccase from Trametes versicolor with Enhanced Stability and Catalytic Activity

Zhang

Chen

et al. 2018

Catalysts

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In this work, laccase from Trametes versicolor pretreated with copper ion solution was entrapped in copper alginate beads. The presence of laccase in copper alginate beads was verified by Fourier transform infrared (FTIR) spectroscopy. The alginate concentration used was optimized based on the specific activity and immobilization yield. After entrapment, laccase presents perfect pH stability and thermal stability with 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) as the substrate. Moreover, laccase in copper alginate beads exhibits good reusability during continuous batch operation for removing 2,4-dichlorophenol. More importantly, owing to the coupled effect of copper ion activation and copper alginate entrapment, the entrapped laccase shows a 3.0-fold and a 2.4-fold increase in specific activity and 2,4-DCP degradation rate compared with that of free laccase, respectively.

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Section: Introductionmentioning

confidence: 99%

An Improved Method to Encapsulate Laccase from Trametes versicolor with Enhanced Stability and Catalytic Activity

Zhang

Chen

et al. 2018

Catalysts

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“…A recent example, Petrovicová et al . co‐immobilized a ketoreductase and a GDH from Bacillus megaterium in polyvinyl alcohol particles and were able to use the derivate 18 times with minimal loss of activity …”

Section: Resultsmentioning

confidence: 99%

Co‐immobilization of P450 BM3 and glucose dehydrogenase on different supports for application as a self‐sufficient oxidative biocatalyst

Solé

Caminal

Schürmann³

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND The oxy‐functionalization of non‐activated carbon bonds by the bacterial cytochrome P450 BM3 from Bacillus megaterium, presents a promising field in biosynthesis and it has gained much interest in recent decades. Nevertheless, the need for the expensive cofactor NADPH, together with low operational stability of the enzyme have made the implementation of this biocatalyst unfeasible in most cases for industry. RESULTS P450 BM3 and glucose dehydrogenase (GDH), as a cofactor regeneration enzyme, were successfully co‐immobilized obtaining a bi‐functional self‐sufficient oxidative biocatalyst. First, a broad screening of 13 different supports was carried out. Five selected agaroses with three different functionalities (epoxy, amine and aldehyde) were studied and their immobilization processes optimized. Finally, P450 BM3 and GDH were co‐immobilized on those supports showing the best performance for P450 BM3 immobilization: epoxy‐agarose (epoxy‐agarose‐UAB) presenting 83% and 20% retained activities respectively; AMINO‐agarose presenting 28% and 25%, and Lentikats® with which both enzymes retained 100% of the initial activity. Furthermore, the re‐utilization of the self‐sufficient immobilized derivatives was tested in five repeated cycles. CONCLUSIONS P450 BM3 and GDH have been successfully immobilized on three supports and their re‐usability has been tested in a model reaction. It represents a step forward for future P450 BM3 industrial implementations. © 2018 Society of Chemical Industry

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“…Such a strategy might overthrow effects deriving from multiple interactions and also mimic "natural" cascade reactions in which enzymes are usually in close proximity to one another [29]. Co-immobilization is frequently used for co-factor-depending enzymes (i.e., oxidoreductases) to fix on the same carrier both the enzyme catalyzing the main biotransformation and an ancillary enzyme responsible for the regeneration of the co-factor [30][31][32][33]. However, due to the complexity of this approach for our case-study, we here opted to have the enzymes immobilized on the same carrier, but separately, for individual optimization, taking advantage from the accumulated data on CpUP, AhPNP and DddAK in the single bioconversions (phosphorolysis, transglycosylation, and phosphorylation) ( Figure S1).…”

Section: Immobilization Carriermentioning

confidence: 99%

A Multi-Enzymatic Cascade Reaction for the Synthesis of Vidarabine 5′-Monophosphate

et al. 2020

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We here described a three-step multi-enzymatic reaction for the one-pot synthesis of vidarabine 5′-monophosphate (araA-MP), an antiviral drug, using arabinosyluracil (araU), adenine (Ade), and adenosine triphosphate (ATP) as precursors. To this aim, three enzymes involved in the biosynthesis of nucleosides and nucleotides were used in a cascade mode after immobilization: uridine phosphorylase from Clostridium perfringens (CpUP), a purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP), and deoxyadenosine kinase from Dictyostelium discoideum (DddAK). Specifically, CpUP catalyzes the phosphorolysis of araU thus generating uracil and α-d-arabinose-1-phosphate. AhPNP catalyzes the coupling between this latter compound and Ade to form araA (vidarabine). This nucleoside becomes the substrate of DddAK, which produces the 5′-mononucleotide counterpart (araA-MP) using ATP as the phosphate donor. Reaction conditions (i.e., medium, temperature, immobilization carriers) and biocatalyst stability have been balanced to achieve the highest conversion of vidarabine 5′-monophosphate (≥95.5%). The combination of the nucleoside phosphorylases twosome with deoxyadenosine kinase in a one-pot cascade allowed (i) a complete shift in the equilibrium-controlled synthesis of the nucleoside towards the product formation; and (ii) to overcome the solubility constraints of araA in aqueous medium, thus providing a new route to the highly productive synthesis of araA-MP.

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Co-Immobilization of Ketoreductase and Glucose Dehydrogenase

Cited by 23 publications

References 23 publications

An Improved Method to Encapsulate Laccase from Trametes versicolor with Enhanced Stability and Catalytic Activity

An Improved Method to Encapsulate Laccase from Trametes versicolor with Enhanced Stability and Catalytic Activity

Co‐immobilization of P450 BM3 and glucose dehydrogenase on different supports for application as a self‐sufficient oxidative biocatalyst

A Multi-Enzymatic Cascade Reaction for the Synthesis of Vidarabine 5′-Monophosphate

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