A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization

Bódalo, A.; Bastida, Jaume; Máximo, M.F.; Montiel, M.C.; Gómez, M.; Murcia, M.D.

doi:10.1007/s00449-008-0207-7

Cited by 58 publications

(28 citation statements)

References 30 publications

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“…Other popular enzymes are horseradish peroxidase and soybean peroxidase: Both enzymes were covalently immobilized onto aldehyde glass through their amine groups, and a clear protective effect of the immobilization against the enzyme inactivation by hydrogen peroxide was found [257,258].…”

Section: Improved Rigidity Of the Enzymementioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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Section: Improved Rigidity Of the Enzymementioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

View full text Add to dashboard Cite

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“…Due to this, it has been used previously in soluble form for removal of aqueous phenols from wastewaters (Flock et al 1999), for synthesis of polyaniline (CruzSilva et al 2005) and as a bromination catalyst (Munir and Dordick 2000). There are only few reports of SHP immobilization studies with alginate (Trivedi et al 2006), glass beads (Bodalo et al 2008) and macroporous glycidyl methacrylate (Prokopijevic et al 2014).…”

Section: Introductionmentioning

confidence: 96%

Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization

Prokopijević

Prodanović

Spasojević

et al. 2016

Appl Microbiol Biotechnol

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Pectin was modified by oxidation with sodium periodate at molar ratios of 2.5, 5, 10, 15 and 20 mol% and reductive amination with tyramine and sodium cyanoborohydride afterwards. Concentration of tyramine groups within modified pectin ranged from 54.5 to 538 μmol/g of dry pectin while concentration of ionizable groups ranged from 3.0 to 4.0 mmol/g of dry polymer compared to 1.5 mmol/g before modification due to the introduction of amino group. All tyramine-pectins showed exceptional gelling properties and could form hydrogel both by cross-linking of carboxyl groups with calcium or by cross-linking phenol groups with peroxidase in the presence of hydrogen peroxide. These hydrogels were tested as carriers for soybean hull peroxidase (SHP) immobilization within microbeads formed in an emulsion based enzymatic polymerization reaction. SHP immobilized within tyramine-pectin microbeads had an increased thermal and organic solvent stability compared to the soluble enzyme. Immobilized SHP was more active in acidic pH region and had slightly decreased K value of 2.61 mM compared to the soluble enzyme. After 7 cycles of repeated use in batch reactor for pyrogallol oxidation microbeads, immobilized SHP retained half of the initial activity.

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“…Such mechanism allows the oxidation of inorganic and organic substrates, including important environmental pollutants such as dyes or polychlorophenols [17][18][19]. In addition, SBP shows a remarkable thermal stability, works well in a wide pH range and has a low sensitivity to various organic solvents [20][21].…”

Section: Introductionmentioning

confidence: 99%