Intensifying the O2-dependent heterogeneous biocatalysis: Superoxygenation of solid support from H2O2 by a catalase tailor-made for effective immobilization

Bolívar, Juan M.; Schelch, Sabine; Pfeiffer, Martin; Nidetzky, Bernd

doi:10.1016/j.molcatb.2016.10.017

Cited by 25 publications

(42 citation statements)

References 31 publications

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“…Catalase (CAT; hydrogen‐peroxide:hydrogen‐peroxide oxidoreductase; EC 1.11.1.6) was used from different sources. One was the commercial enzyme from bovine liver ( Bl CAT; Sigma‐Aldrich), the other was from Bordetella pertussis ( Bp CAT) and was obtained as a N‐terminal fusion protein with Z basic2 (Bolivar, Schelch, Pfeiffer, & Nidetzky, ). Note that Bl CAT and Bp CAT were chosen in consideration of the planned coimmobilization of oxidase and CAT.…”

Section: Methodsmentioning

confidence: 99%

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Process intensification for O₂‐dependent enzymatic transformations in continuous single‐phase pressurized flow

Bolívar

Mannsberger

Thomsen

et al. 2019

Biotech & Bioengineering

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Oxidative O 2 ‐dependent biotransformations are promising for chemical synthesis, but their development to an efficiency required in fine chemical manufacturing has proven difficult. General problem for process engineering of these systems is that thermodynamic and kinetic limitations on supplying O 2 to the enzymatic reaction combine to create a complex bottleneck on conversion efficiency. We show here that continuous‐flow microreactor technology offers a comprehensive solution. It does so by expanding the process window to the medium pressure range (here, ≤34 bar) and thus enables biotransformations to be conducted in a single liquid phase at boosted concentrations of the dissolved O 2 (here, up to 43 mM). We take reactions of glucose oxidase and d ‐amino acid oxidase as exemplary cases to demonstrate that the pressurized microreactor presents a powerful engineering tool uniquely apt to overcome restrictions inherent to the individual O 2 ‐dependent transformation considered. Using soluble enzymes in liquid flow, we show reaction rate enhancement (up to six‐fold) due to the effect of elevated O 2 concentrations on the oxidase kinetics. When additional catalase was used to recycle dissolved O 2 from the H 2 O 2 released in the oxidase reaction, product formation was doubled compared to the O 2 supplied, in the absence of transfer from a gas phase. A packed‐bed reactor containing oxidase and catalase coimmobilized on porous beads was implemented to demonstrate catalyst recyclability and operational stability during continuous high‐pressure conversion. Product concentrations of up to 80 mM were obtained at low residence times (1–4 min). Up to 360 reactor cycles were performed at constant product release and near‐theoretical utilization of the O 2 supplied. Therefore, we show that the pressurized microreactor is practical embodiment of a general reaction‐engineering concept for process intensification in enzymatic conversions requiring O 2 as the cosubstrate.

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Section: Methodsmentioning

confidence: 99%

“…DAAO and BpCAT were coimmobilized on Relsulfonate. Previously reported procedure (Bolivar, Schelch, et al, 2016) was used. The DAAO was immobilized before the BpCAT.…”

Section: Immobilizationmentioning

confidence: 99%

Process intensification for O₂‐dependent enzymatic transformations in continuous single‐phase pressurized flow

Bolívar

Mannsberger

Thomsen

et al. 2019

Biotech & Bioengineering

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“…D-Amino acid oxidase from Trigonopsis variabilis (DAAO) 45,56 and catalase (CATA) from 19,48 were used. Each enzyme was obtained in a chimeric form that had the Z basic2 module fused at the N-terminus 47,48 .…”

Section: Enzymesmentioning

confidence: 99%

“…Due to the extremely high specific activity of the catalase, its activity is normally present in large excess. 48 The task thus becomes to immobilize a maximum amount of oxidase (here: D-amino acid oxidase) and to make sure that the O 2 demand of the oxidase is partly fulfilled from the catalase reaction via effective hydrogen peroxide degradation. Variation in overall silica morphology as well as in OMSM pore structural framework was used in synthetic silica materials to explore material characteristics important for efficiency in the co-immobilization of the two enzymes.…”

Section: Introductionmentioning

confidence: 99%

Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica

et al. 2017

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Mesoporous silica materials are promising carriers for enzyme immobilization in heterogeneous biocatalysis applications. By tailoring their pore structural framework, these materials are designable for appropriate enzyme binding capacity and internal diffusivity. To supply O 2 efficiently to solid-supported immobilized enzymes represents a core problem of heterogeneously catalyzed oxidative biotransformations. In this study, therefore, we synthesized and compared three internally well-ordered and two amorphous silica materials as enzyme carriers, each of those with pore sizes of ≥10 nm, to enable the co-immobilization of D-aminoacid oxidase (93 kDa) and catalase (245 kDa). Both enzymes were fused to the silica-binding module Z basic2 to facilitate their selective and oriented immobilization directly from crude protein mixtures on native silica materials. Analyzing the effects of varied pore architecture and internal surface area on the performance of the immobilized bienzymatic system, we showed that a uniform pore structural framework was beneficial for enzyme loading (≥ 70 mg protein/g carrier), immobilization yield (≥ 90%), surface and pore volume filling without hindered adsorption, and catalytic effectiveness (≥ 60%) of the co-immobilizate. Using the best carrier LP-SBA-15, we obtained a solid oxidase-catalase preparation with an activity of 2000 µmol/(min g_material) that was recyclable and stable during oxidation of D-methionine. These results affirm a strategy of optimizing immobilized O 2 -dependent enzymes via tunable internal structuring of the silica material used as carrier. They thus make a significant advance towards the molecular design of heterogeneous oxidation biocatalysts on mesoporous silica supports.

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“…CAT catalyzes hydrogen peroxide disproportionation to release water and molecular oxygen as innocuous products . Such a catalytic reaction makes this enzyme industrially relevant for the development of biosensors, preventing food oxidation, removing hydrogen peroxide from residual water, and the intensification of oxidase‐driven biotransformations . In a pioneering attempt to expand the applications of CAT, our group has recently exploited CAT in solution to produce bubbles upon H 2 O 2 disproportionation as a source of mechanical energy, which is then harvested by coupling to piezoelectric materials to generate electricity .…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic Protein‐Based Materials for Integration into Energy Devices

et al. 2019

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There is a current need to fabricate new biobased functional materials. Bottom‐up approaches to assemble simple molecular units have shown promise for biomaterial fabrication due to their tunability and versatility for the incorporation of functionalities. Herein, the fabrication of catalytic protein thin films by the entrapment of catalase into protein films composed of a scaffolding protein is demonstrated. Extensive structural and functional characterization of the films provide evidence of the structural integrity, order, stability, catalytic activity, and reusability of the biocatalytic materials. Finally, these functional biomaterials are coupled with piezoelectric disks to fabricate a second generation of bio‐inorganic generators. These devices are capable of producing electricity from renewable fuels through catalase‐driven gas production that mechanically stimulates the piezoelectric material.

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Intensifying the O2-dependent heterogeneous biocatalysis: Superoxygenation of solid support from H2O2 by a catalase tailor-made for effective immobilization

Cited by 25 publications

References 31 publications

Process intensification for O₂‐dependent enzymatic transformations in continuous single‐phase pressurized flow

Process intensification for O₂‐dependent enzymatic transformations in continuous single‐phase pressurized flow

Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica

Biocatalytic Protein‐Based Materials for Integration into Energy Devices

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Intensifying the O2-dependent heterogeneous biocatalysis: Superoxygenation of solid support from H2O2 by a catalase tailor-made for effective immobilization

Cited by 25 publications

References 31 publications

Process intensification for O2‐dependent enzymatic transformations in continuous single‐phase pressurized flow

Process intensification for O2‐dependent enzymatic transformations in continuous single‐phase pressurized flow

Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica

Biocatalytic Protein‐Based Materials for Integration into Energy Devices

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Process intensification for O₂‐dependent enzymatic transformations in continuous single‐phase pressurized flow

Process intensification for O₂‐dependent enzymatic transformations in continuous single‐phase pressurized flow