Noncovalent immobilization of chloroperoxidase onto talc: Catalytic properties of a new biocatalyst

Aoun, Salim; Chebli, C.; Baboulène, M.

doi:10.1016/s0141-0229(98)00061-1

Cited by 25 publications

(18 citation statements)

References 25 publications

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“…For example, the use of CPO immobilized on microporous talc in bromohydroxylation reactions was reported [25]. Higher regioselectivities and improved oxidative stability were found for the immobilized enzyme.…”

Section: Immobilization On Inorganic Supportsmentioning

confidence: 99%

See 1 more Smart Citation

Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification

Longoria

Tinoco

Torres

2010

Biocatalysis Based on Heme Peroxidases

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Section: Immobilization On Inorganic Supportsmentioning

confidence: 99%

“…In contrast to the hydrophobic talc (15M00), the hydrophilic talc (CLST) was less favorable to adsorption ( 2.5 mg CPO/g talc); however, the CLST-CPO combination had excellent enzymatic activity (80-126%) [25] Immobilized HRP on gelatin in presence of NaY zeolite…”

Section: Introductionmentioning

confidence: 99%

Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification

Longoria

Tinoco

Torres

2010

Biocatalysis Based on Heme Peroxidases

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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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“…8 So, a lot of methods have been developed to enhance the CPO activity and its thermal stability, such as increasing the initial enzymatic activity in reverse micellar systems, 9 microencapsulating CPO as a recyclable catalyst, 10 and immobilizing CPO on some mesoporous or macromolecular materials. [11][12][13][14] In this work, the effects of metal ions on CPO chlorination activity at 25 ℃ and at elevated temperatures were investigated. The result indicated that Ca 2＋ , Mg 2＋ , Co 2＋ , and Ni 2＋ could enhance chlorination activity of CPO at 25 ℃, and meanwhile, they could also improve the CPO thermal stability in a temperature range from 35 to 55 ℃.…”

Section: Introductionmentioning

confidence: 99%

Activation Function of Chloroperoxidase in the Presence of Metal Ions at Elevated Temperature from 25 to 55°C

Gao¹,

Jiang²,

Gao³

et al. 2009

Chin. J. Chem.

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The investigation and comparison of chlorination activity of chloroperoxidase (CPO) from Caldariomyces fumago in metal ion solutions to those in pure buffer indicated that CPO could be effectively activated by some alkaline-earth metals and transition metals. Glu183, His105 and Asp106 around the active site of CPO, and activate CPO by both an enrichment of substrate concentration and the conformational change of CPO, which are favorable to the substrate access. The analysis of kinetic parameters indicated that the activation was mainly due to an increase in k cat values. The affinity and specificity of CPO to substrates were also improved in these metal ion media. The results in this work are promising in view of industrial applications of this versatile biological catalyst.

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Noncovalent immobilization of chloroperoxidase onto talc: Catalytic properties of a new biocatalyst

Cited by 25 publications

References 25 publications

Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification

Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification

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

Activation Function of Chloroperoxidase in the Presence of Metal Ions at Elevated Temperature from 25 to 55°C

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