Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors

Hoog, H.; Nallani, Madhavan; Cornelissen, Jeroen J. L. M.; Rowan, Alan E.; Nolte, Roeland J. M.; Arends, Isabel W. C. E.

doi:10.1039/b911370c

Cited by 37 publications

(23 citation statements)

References 50 publications

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“…Alginate‐ graft ‐poly(ethylene glycol)/α‐cyclodextrin (Alg‐g‐PEG/α‐CD) vesicles are permeable to L ‐asparagine, but not to the encapsulated enzyme L‐asparaginase 140. Other known permeable polymersomes are based on PS‐ b ‐PIAT 133, 141–145, on oppositely charged copolymers comprising a peptide block,146, 147 or on serum albumin‐PS giant amphiphiles 148. The poly(2‐methyl‐2‐oxazoline)‐ block ‐poly(dimethyl siloxane)‐ block ‐poly(2‐methyl‐2‐oxazoline) (PMOXA‐ b ‐PDMS‐ b ‐PMOXA) polymersome membrane is known to be impermeable to calcium ions149 and almost impermeable to water 150.…”

Section: Synthetic Nanoreactorsmentioning

confidence: 99%

Selective and Responsive Nanoreactors

Renggli

Baumann

Langowska

et al. 2011

Adv Funct Materials

228

242

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Chemical reactions can be confi ned to nanoscale compartments by encapsulating catalysts in hollow nanoobjects. Such reaction compartments effectively become nanoreactors when substrate and product are exchanged between bulk solution and cavity. A key issue, thereby, is control of shell permeability. Nanoreactors exhibit selectivity and responsiveness if their shells discriminate among molecules and if access can be modulated by external triggers. Here, we review natural nanoreactors that include protein-based bacterial microcompartments, protein cages, and viruses. Artifi cial nanoreactors based on dendrimers, layer-by-layer capsules, and amphiphilic block copolymer polymersomes are also discussed. Selectivity in these nanoreactors is either due to intrinsic reactor-shell semipermeability or can be engineered using smart polymers to gate the reactors. Moreover, a rich repertoire of pores and channels are already provided in nature, e.g., in protein-based nanoreactors or in trans-membrane channel proteins. The latter can be reconstituted in polymersomes, resulting in gated vesicles. Nanoreactors hold promise for applications ranging from selective and size-constrained organic synthesis to biomedical advances (e.g., artifi cial organelles, biosensing) and as analytical tools to study reaction mechanisms.

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Section: Synthetic Nanoreactorsmentioning

confidence: 99%

Selective and Responsive Nanoreactors

Renggli

Baumann

Langowska

et al. 2011

Adv Funct Materials

228

242

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“…On the other hand, there are a large number of reports regarding CPO immobilization [for representative examples, see [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25], showing a broad range of enzyme load and retained activity. Reported immobilization techniques range from the use of typical methods such as physical adsorption onto mesoporous materials, talc, and others to the combination of several methods such as CLEA's entrapment in mesoporous materials.…”

Section: Introductionmentioning

confidence: 99%

Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase

Salcedo¹,

Torres

Haces

et al. 2015

Biocatalysis

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Chloroperoxidase fromCaldariomyces fumago was immobilized in Eupergit ® C, a commercial mesoporous acrylic-based material. Due to low stability of the enzyme under neutral and basic pH, the usual covalent immobilization procedures cannot be applied to this enzyme. Several strategies were followed in order to achieve a stable interaction between the protein and the support. The support was efficiently functionalized with different reactive groups such as aromatic and aliphatic amines, glutaraldehyde, diazonium ions, and maleimide moieties; solvent-exposed amino acid residues in chloroperoxidase were identified or created through chemical modification, so that they were reactive under conditions where the enzyme is stable. Enzyme load and retained activity were monitored, obtaining biocatalysts with specific activity ranging from 200 to 25,000 U/g. The highest load and activity was obtained from the immobilization of a chemically-modified CPO preparation bearing a solvent-exposed free thiol group. This biocatalyst efficiently catalyzed the transformation of β-estradiol, an endocrine disruptor.

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“…The immobilization of CPO on silica gel [18,34,43,51], talc [2], mesoporous materials [1, 6, 23-25, 30, 50, 52], and magnetic particles [5,21,56] was demonstrated to increase its tolerance to organic solvent, elevated temperature, and low pH. Genetic manipulation of CPO through random mutagenesis [54] and directed evolution [28,44,58,59] could result in variants with enhanced specific activity.…”

Section: Introductionmentioning

confidence: 99%

Activity and Stability of Chloroperoxidase in the Presence of Small Quantities of Polysaccharides: A Catalytically Favorable Conformation Was Induced

Wang

Jiang

et al. 2011

Appl Biochem Biotechnol

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Chloroperoxidase (CPO) is thought to be the most versatile heme-containing enzyme with enormous applications in organic synthesis, biotransformation, pharmaceutical production, and detoxification of environmental pollutants. Any improvement in the stability of this enzyme will greatly enhance its application in the mentioned areas. In the present study, the effects of three polysaccharides (soluble starch, β-cyclodextrin, and dextrin) on the stability of CPO at elevated temperatures (20, 30, 35, 40, and 50 °C) or in aqueous-organic solvents media (methanol, dioxane, DMSO, and DMF) were investigated. An improved catalytic performance of CPO was observed in the presence of a small amount of the three polysaccharides, where dextrin provided the most effective promotion. The changes of enzyme structure and microenvironment around heme in the presence of additives were studied by fluorescence, circular dichroism, and UV-vis spectra analyses, as well as kinetic parameters measurement. A catalytically favorable structure of CPO was induced, including the strengthening of the α-helix structure and more exposure of heme for easy access of the substrate, resulting in an increase of catalytic turnover frequency (k (cat)) and the improvement of affinity and selectivity of CPO to substrate. The results revealed that the introduction of trace soluble starch, β-cyclodextrin, and dextrin (<10 μmol/L) in reaction media was an effective strategy for the enhancement of the thermodynamic and the operational stability of the enzyme, which are promising in view of the industrial applications of this versatile biological catalyst.

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Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors

Cited by 37 publications

References 50 publications

Selective and Responsive Nanoreactors

Selective and Responsive Nanoreactors

Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase

Activity and Stability of Chloroperoxidase in the Presence of Small Quantities of Polysaccharides: A Catalytically Favorable Conformation Was Induced

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