Combined cross-linked enzyme aggregates of horseradish peroxidase and glucose oxidase for catalyzing cascade chemical reactions

Nguyen, Le Truc; Yang, Kun‐Lin

doi:10.1016/j.enzmictec.2017.02.007

Cited by 83 publications

(62 citation statements)

References 36 publications

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“…A combi-CLEA consisting of glucose oxidase and horse radish peroxidase (HRP) can be used for the in situ production of hydrogen peroxide by aerobic oxidation of glucose followed by HRP catalyzed oxidations with the hydrogen peroxide [147]. Similarly, a combi-CLEA consisting of glucose oxidase and versatile peroxide (VP), with added glucose, catalyzed the elimination of endocrine disruptors from industrial wastewater streams [148].…”

Section: Multi-and Combi-cleasmentioning

confidence: 99%

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

2019

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Biocatalysis has emerged in the last decade as a pre-eminent technology for enabling the envisaged transition to a more sustainable bio-based economy. For industrial viability it is essential that enzymes can be readily recovered and recycled by immobilization as solid, recyclable catalysts. One method to achieve this is via carrier-free immobilization as cross-linked enzyme aggregates (CLEAs). This methodology proved to be very effective with a broad selection of enzymes, in particular carbohydrate-converting enzymes. Methods for optimizing CLEA preparations by, for example, adding proteic feeders to promote cross-linking, and strategies for making the pores accessible for macromolecular substrates are critically reviewed and compared. Co-immobilization of two or more enzymes in combi-CLEAs enables the cost-effective use of multiple enzymes in biocatalytic cascade processes and the use of "smart" magnetic CLEAs to separate the immobilized enzyme from other solids has raised the CLEA technology to a new level of industrial and environmental relevance. Magnetic-CLEAs of polysaccharide-converting enzymes, for example, are eminently suitable for use in the conversion of first and second generation biomass.Catalysts 2019, 9, 261 2 of 31 and deprotection steps. This affords synthetic routes that, compared with conventional organic syntheses, are more step economic, more energy efficient, generate less waste and provide products in exquisite stereochemical purities that are difficult to compete with.Consequently, in the last two decades biocatalysis has emerged as an important technology for meeting the growing demand for green and sustainable processing [2][3][4]. This embraces the whole gamut of chemicals manufacture, from the enantioselective synthesis of chiral drugs [5][6][7][8][9][10][11][12] to the conversion of renewable biomass to liquid fuels and commodity chemicals [13][14][15]. This raises the perennial question: if biocatalysis is so superior why has it not been extensively used in the past? The answer is simple: thanks to advances in molecular biology and biotechnology, biocatalysis has undergone a spectacular leap forward in the last two decades:-Many more enzymes have been identified through (meta)genome mining, that is the in silico analysis of publicly accessible genome sequence data bases that have been generated as a result of next generation genome sequencing [16]. -Advances in gene synthesis have enabled the synthesis of identified genes, ready for cloning into a host production organism, in a few weeks at relatively low cost. This has significantly reduced the cost of development and subsequent production of enzymes at industrial scale. -Advances in protein engineering, using directed evolution techniques [17,18], have enabled optimization of enzyme performance under the challenging conditions encountered in industrial-scale processes, namely, high (stereo)selectivities, activities and space-time yields with non-natural substrates at high substrate concentrations, in the presence of organic solve...

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Section: Multi-and Combi-cleasmentioning

confidence: 99%

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

2019

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“…As discussed above, many scaffolds, abiotic and biotic, are available [4]. The influence of scaffold material is illustrated by the effect of DNA on the coupled reaction of horseradish peroxidase (HRP) and glucose oxidase (GOx), which oxidizes glucose to D-glucono-δ-lactone and H 2 O 2 then uses H 2 O 2 to oxidize dyes such as 2,2 -azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) [21,[72][73][74]. When HRP and GOx were scaffolded onto negatively-charged DNA, the rate of the coupled reaction increased several fold, and this changed with distance between the enzymes.…”

Section: Factors Affecting Immobilization Benefits-immobilization Chementioning

confidence: 99%

Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

et al. 2020

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Nanoparticle scaffolds can impart multiple benefits onto immobilized enzymes including enhanced stability, activity, and recoverability. The magnitude of these benefits is modulated by features inherent to the scaffold–enzyme conjugate, amongst which the size of the nanoscaffold itself can be critically important. In this review, we highlight the benefits of enzyme immobilization on nanoparticles and the factors affecting these benefits using quantum dots and gold nanoparticles as representative materials due to their maturity. We then review recent literature on the use of these scaffolds for enzyme immobilization and as a means to dissect the underlying mechanisms. Detailed analysis of the literature suggests that there is a “sweet-spot” for scaffold size and the ratio of immobilized enzyme to scaffold, with smaller scaffolds and lower enzyme:scaffold ratios generally providing higher enzymatic activities. We anticipate that ongoing studies of enzyme immobilization onto nanoscale scaffolds will continue to sharpen our understanding of what gives rise to beneficial characteristics and allow for the next important step, namely, that of translation to large-scale processes that exploit these properties.

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“…A general problem associated with CLEAs is the existence of strong substrate diffusional limitations, mainly if the enzyme activity is very high or when using large substrates. In this sense, another positive effect of using dexOx instead of glutaraldehyde is the generation of larger pores, therefore reducing these substrate diffusional problems [205][206][207][208]. For instance, CLEAs of β-mannanase were prepared using dexOx; scanning electron microscopy confirmed the porous structure with low steric hindrances, leading to a 16-fold increase of the enzymatic activity when compared to the CLEA crosslinked with glutaraldehyde [209].…”

Section: Dextran Aldehyde In the Preparation Of Crosslinked Enzyme Agmentioning

confidence: 99%

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

et al. 2019

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Dextran aldehyde (dexOx), resulting from the periodate oxidative cleavage of 1,2-diol moiety inside dextran, is a polymer that is very useful in many areas, including as a macromolecular carrier for drug delivery and other biomedical applications. In particular, it has been widely used for chemical engineering of enzymes, with the aim of designing better biocatalysts that possess improved catalytic properties, making them more stable and/or active for different catalytic reactions. This polymer possesses a very flexible hydrophilic structure, which becomes inert after chemical reduction; therefore, dexOx comes to be highly versatile in a biocatalyst design. This paper presents an overview of the multiple applications of dexOx in applied biocatalysis, e.g., to modulate the adsorption of biomolecules on carrier surfaces in affinity chromatography and biosensors design, to serve as a spacer arm between a ligand and the support in biomacromolecule immobilization procedures or to generate artificial microenvironments around the enzyme molecules or to stabilize multimeric enzymes by intersubunit crosslinking, among many other applications.

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Combined cross-linked enzyme aggregates of horseradish peroxidase and glucose oxidase for catalyzing cascade chemical reactions

Cited by 83 publications

References 36 publications

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

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