Process intensification in oxidative biocatalysis

Vernet, Guillem; Hobisch, Markus; Kara, Selin

doi:10.1016/j.cogsc.2022.100692

Cited by 10 publications

(13 citation statements)

References 65 publications

(39 reference statements)

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“…Using organic solvent has been reported as a good alternative for process intensification of biocatalysis and can avoid water‐related issues [38] . In particular, various studies have demonstrated that performing the established cascade in water‐deficient media could largely minimize the auto‐hydrolysis of ECL [4,31,53] .…”

Section: Resultsmentioning

confidence: 99%

“…Using organic solvent has been reported as a good alternative for process intensification of biocatalysis and can avoid waterrelated issues. [38] In particular, various studies have demonstrated that performing the established cascade in waterdeficient media could largely minimize the auto-hydrolysis of ECL. [4,31,53] In this study, three organic solvents, 2-methyltetrahydrofuran (2-MeTHF), methyl tert-butyl ether (MTBE), and cyclopentyl methyl ether (CPME), have been selected because of their sustainability and reported prospective results.…”

Section: Clea Catalysis In a Microaqueous Organic Systemmentioning

confidence: 99%

“…Especially, enzyme immobilization technique is a common strategy to mitigate the loss of stability under storage and operational conditions. In addition, it allows for the easy recovery and reusability of biocatalysts in batch or continuous operation systems while increasing stability against high temperatures and co‐solvents [38–43] . Most isolated BVMOs have been immobilized by covalent binding to polymeric supports [2] .…”

Section: Introductionmentioning

confidence: 99%

“…In addition, it allows for the easy recovery and reusability of biocatalysts in batch or continuous operation systems while increasing stability against high temperatures and co-solvents. [38][39][40][41][42][43] Most isolated BVMOs have been immobilized by covalent binding to polymeric supports. [2] However, the chemical bond formed between enzymes and carriers might distort enzyme structures, leading to reduced activity, whilst the use of carriers is sometimes costlier.…”

Section: Introductionmentioning

confidence: 99%

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Crosslinked Aggregates of Fusion Enzymes in Microaqueous Organic Media

2023

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Baeyer-Villiger monooxygenases (BVMOs) are attractive for selectively oxidizing various ketones using oxygen into valuable esters and lactones. However, the application of BVMOs is restrained by cofactor dependency and enzyme instability combined with water-related downsides such as low substrate loading, low oxygen capacity, and water-induced side reactions. Herein, we described a redox-neutral linear cascade with in-situ cofactor regeneration catalyzed by fused alcohol dehydrogenase and cyclohexanone monooxygenase in aqueous and microaqueous organic media. The cascade conditions have been optimized regarding substrate concentrations as well as the amounts of enzymes and cofactors with the Design of Experiments (DoE). The carrier-free immobilization technique, crosslinked enzyme aggregates (CLEAs), was applied to fusion enzymes. The resultant fusion CLEAs were proven to function in microaqueous organic systems, in which the enzyme ratios, water contents (0.5-5 vol. %), and stability have been systematically studied. The fusion CLEAs showed promising operational (up to 5 cycles) and storage stability.

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Section: Resultsmentioning

confidence: 99%

Section: Clea Catalysis In a Microaqueous Organic Systemmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Crosslinked Aggregates of Fusion Enzymes in Microaqueous Organic Media

2023

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“…However, the practical utilization of GalOx is often hindered by inherent biochemical limitations. One primary limitation is its dependency on oxygen (O 2 ), which may restrict its effectiveness under specific operational conditions [9–13] . The availability of oxygen plays a crucial role in achieving productive reactions catalyzed by GalOx, necessitating efficient and rapid oxygen supply [11–14] .…”

Section: Introductionmentioning

confidence: 99%

Overcoming Biochemical Limitations of Galactose Oxidase through the Design of a Solid‐Supported Self‐Sufficient Biocatalyst

Lorente‐Arevalo,

Orellana,

Ladero

et al. 2023

ChemBioChem

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Galactose Oxidase (GalOx) has gained significant interest in biocatalysis due to its ability for selective oxidation beyond the natural oxidation of galactose. However, the practical application of GalOx has been hindered by the limited availability of active and stable biocatalysts, as well as the inherent biochemical limitations such as oxygen (O2) dependency and the need for activation. In this study, we addressed these challenges by immobilizing GalOx into agarose‐based and Purolite supports. Additionally, we identified and quantified the oxygen supply limitation into solid catalysts by intraparticle oxygen sensing showing a trade‐off between the amount of protein loaded onto the solid support and the catalytic effectiveness. Furthermore, we coimmobilized a heme‐containing protein along with the enzyme to function as an activator. To evaluate the application of the immobilized GalOx, we conducted the oxidation of galactose in an instrumented aerated reactor. The results showcased the efficient performance of the immobilized enzyme in the 8 h reaction cycle. Notably, the GalOx immobilized into dextran sulfate‐activated agarose exhibited improved stability, overcoming the need for a soluble activator supply, and demonstrated exceptional performance in galactose oxidation. These findings offer promising prospects for the utilization of GalOx in technical biocatalytic applications.

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Current Advances in the Enzyme Engineering of O₂‐Dependent Enzymes – Boosting the Versatility and Applicability of Oxygenases and Oxidases

Al‐Shameri,

Schmermund,

Sieber

2024

ChemCatChem

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Oxidation reactions catalyzed by O2‐dependent enzymes are gaining increasing interest in the chemical industry due to their potential to provide a more selective, benign and sustainable alternative to the conventional chemical oxidation methods. O2‐dependent enzymes, like oxidases and oxygenases, catalyze a versatile range of oxidative reactions using only molecular oxygen as oxidant. However, their practical application on larger scale has been limited up to this point, primarily due to factors like their low catalytic rates combined by a narrow substrate spectrum and low stability. Nonetheless, in recent years, enzyme engineering studies have made significant progress in addressing these challenges and moving O2‐dependent enzymes closer towards industrial utilization. In this review, we aim to provide a concise overview of the most recent engineering approaches on O2‐dependent enzymes. We will highlight recent studies that have targeted various aspects of O2‐dependent enzymes including, activity, selectivity, stability, and substrate spectrum with a focus on engineering studies where the engineered enzymes catalyze synthetically valuable reactions.

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Process intensification in oxidative biocatalysis

Cited by 10 publications

References 65 publications

Crosslinked Aggregates of Fusion Enzymes in Microaqueous Organic Media

Crosslinked Aggregates of Fusion Enzymes in Microaqueous Organic Media

Overcoming Biochemical Limitations of Galactose Oxidase through the Design of a Solid‐Supported Self‐Sufficient Biocatalyst

Current Advances in the Enzyme Engineering of O₂‐Dependent Enzymes – Boosting the Versatility and Applicability of Oxygenases and Oxidases

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Process intensification in oxidative biocatalysis

Cited by 10 publications

References 65 publications

Crosslinked Aggregates of Fusion Enzymes in Microaqueous Organic Media

Crosslinked Aggregates of Fusion Enzymes in Microaqueous Organic Media

Overcoming Biochemical Limitations of Galactose Oxidase through the Design of a Solid‐Supported Self‐Sufficient Biocatalyst

Current Advances in the Enzyme Engineering of O2‐Dependent Enzymes – Boosting the Versatility and Applicability of Oxygenases and Oxidases

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Product

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Current Advances in the Enzyme Engineering of O₂‐Dependent Enzymes – Boosting the Versatility and Applicability of Oxygenases and Oxidases