Vanadate(<scp>v</scp>)-dependent bromoperoxidase immobilized on magnetic beads as reusable catalyst for oxidative bromination

Wischang, Diana; Hartung, Jens; Hahn, Thomas; Ulber, Roland; Stumpf, Tobias; Fecher‐Trost, Claudia

doi:10.1039/c0gc00499e

Cited by 26 publications

(12 citation statements)

References 26 publications

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“…From biomimetic chemistry point of view, such reactions are very important as functional models where the ligated vanadate ion oxidizes halide ions in the presence of oxidant such as H 2 O 2 to produce hypohalous acid (HOX) which are chemically equivalent to an electrophilic “X + ” [4] . During oxidative bromination, as observed in enzymatic system as well as functional models, an oxido(peroxido)vanadium(V) species forms which allows nucleophilic attack of the bromide ion, followed by release of HOBr/Br 2 which actually brominates the substrates [5–9] . A good number of research papers dealing with ‘‘green” procedures for introducing bromo group(s) into organic molecules, [10–13] a reaction of primary synthetic and industrial importance, has been analysed by many research groups [1–13] .…”

Section: Introductionmentioning

confidence: 99%

Selective Bromination of β‐Positions of Porphyrin by Self‐Catalytic Behaviour of VOTPP: Facile Synthesis, Electrochemical Redox Properties and Catalytic Application

et al. 2021

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Oxidovanadium(IV) complex of β‐octabromo‐meso‐tetraphenylporphyrin, {[VIVO(TPPBr8)], 2} was synthesized by self‐catalytic oxidative bromination of meso‐tetraphenylporphyrinatooxidovanadium(IV) {[VIVO(TPP), 1} in excellent yield under mild conditions at 25 °C and its structure was confirmed by single crystal X‐ray study. UV‐Vis and 1H NMR spectra further confirmed that the meso‐phenyl rings are not brominated and thus emphasizes on the selectivity as well as synthetic importance of this catalytic method. In the presence of substrates e. g. phenol derivatives, 1 biomimics the vanadium bromoperoxidase (VBPO) enzyme and catalyses the oxidative bromination of substrates in water at 25 °C. Remarkably, 2 also catalyses the oxidative bromination of phenol derivatives under similar reaction conditions with very high turnover frequency (TOF) values (ca. 29 s−1) along with its recyclability. It was found that 2 showed superior catalytic performance as compared to 1 because of its electron deficient nature due to electron withdrawing bromo substituents and robust saddle shaped nonplanar structure (further supported by DFT studies).

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Section: Introductionmentioning

confidence: 99%

Selective Bromination of β‐Positions of Porphyrin by Self‐Catalytic Behaviour of VOTPP: Facile Synthesis, Electrochemical Redox Properties and Catalytic Application

et al. 2021

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“…Chitin, chitosan, activated silica and glass nanoparticles have been used as supports for enzyme immobilization 9 – 12 . It is worth mentioning that a core-shell structured iron oxide magnetic nanoparticle was used to immobilize Thermomyces lanuginosus lipase 13 . Biological reactions using immobilized enzyme can enable the easy separation of the enzyme from the product, the multiple reuses of enzyme, and a high operational stability, as well as the low cost of enzymes 14 .…”

Section: Introductionmentioning

confidence: 99%

Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis

Gong

Zhu

et al. 2017

Sci Rep

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Enzymatic catalysis in microreactors has attracted growing scientific interest because of high specific surface enabling heat and mass transfer and easier control of reaction parameters in microreactors. However, two major challenges that limit their application are fast inactivation and the inability to the biocatalysts in microchannel reactors. A fluid and unsinkable immobilized enzyme were firstly applied in a microchannel reactor for biocatalysis in this study. Functionalized forms of graphene-immobilized naringinase flowing in microchannels have yielded excellent results for isoquercitrin production. A maximum yield of 92.24 ± 3.26% was obtained after 20 min in a microchannel reactor. Ten cycles of enzymatic hydrolysis reaction were successively completed and an enzyme activity above 85.51 ± 2.76% was maintained. The kinetic parameter V m/K m increased to 1.9-fold and reaction time was decreased to 1/3 compared with that in a batch reactor. These results indicated that the moving and unsinkable graphene sheets immobilized enzyme with a high persistent specificity and a mild catalytic characteristic enabled the repetitive use of enzyme and significant cost saving for the application of enzyme catalysis. Thus, the developed method has provided an efficient and simple approach for the productive and repeatable microfluidic biocatalysis.

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“…Depending on the substrate range, it is conceivable that this enzymatic process could be applied to more complex mixtures of amino acids such as hydrolysate of protein-rich waste streams. Immobilizing the enzyme on a solid support [19,20] may allow recyclability and scale-up.…”

mentioning

confidence: 99%

Selective Oxidative Decarboxylation of Amino Acids to Produce Industrially Relevant Nitriles by Vanadium Chloroperoxidase

et al. 2012

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Industrial nitriles from biomass: Vanadium-chloroperoxidase is successfully used to transform selectively glutamic acid into 3-cyanopropanoic acid, a key intermediate for the synthesis of bio-succinonitrile and bio-acrylonitrile, by using a catalytic amount of a halide salt. This clean oxidative decarboxylation can be applied to mixtures of amino acids obtained from plant waste streams, leading to easily separable nitriles.

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Vanadate(v)-dependent bromoperoxidase immobilized on magnetic beads as reusable catalyst for oxidative bromination

Cited by 26 publications

References 26 publications

Selective Bromination of β‐Positions of Porphyrin by Self‐Catalytic Behaviour of VOTPP: Facile Synthesis, Electrochemical Redox Properties and Catalytic Application

Selective Bromination of β‐Positions of Porphyrin by Self‐Catalytic Behaviour of VOTPP: Facile Synthesis, Electrochemical Redox Properties and Catalytic Application

Moving and unsinkable graphene sheets immobilized enzyme for microfluidic biocatalysis

Selective Oxidative Decarboxylation of Amino Acids to Produce Industrially Relevant Nitriles by Vanadium Chloroperoxidase

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