Enhanced catalytic performance and stability of chloroperoxidase from Caldariomyces fumago in surfactant free ternary water–organic solvent systems

Tzialla, Aikaterini A.; Kalogeris, Emmanuel; Gournis, Dimitrios; Sanakis, Yiannis; Stamatis, Haralambos

doi:10.1016/j.molcatb.2007.10.006

Cited by 36 publications

(44 citation statements)

References 62 publications

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“…[20] The use of tert-butylhydroperoxide (TBHP) in the place of H 2 O 2 has proven successful in some cases. [21] In other strategies, polymers [22] and antioxidants [23] were added, or co-solvents such as an ionic liquid [24,25] or ternary systems [26] were employed. Immobilization of haloperoxidases on solid supports did increase the stability of the enzyme and facilitated its recovery.…”

Section: Biological Halogenation and Biomimeticsmentioning

confidence: 99%

Oxidative Halogenation with “Green” Oxidants: Oxygen and Hydrogen Peroxide

2009

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It is difficult to imagine organic chemistry without organo-halogen compounds and the molecular halogens needed for their preparation. The halogens have very different reactivity, with iodine usually requiring some form of activation, while others are reactive and hazardous chemicals. To avoid their use, various modified reagents have been discovered (N-bromo- and N-chlorosuccinimide, Selectfluor..), but halogens are used to prepare these reagents and when they are used the atom economy is poor. A better approach, which is based on biomimetric research on oxidative halogenation in nature, consists of generating the halogenating reagent in situ under acidic conditions from a halide salt. The result of such a reaction has been halogenation with 100 % halogen atom economy. Suitable oxidants for the oxidation of halides are hydrogen peroxide and oxygen.

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Section: Biological Halogenation and Biomimeticsmentioning

confidence: 99%

Oxidative Halogenation with “Green” Oxidants: Oxygen and Hydrogen Peroxide

2009

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“…In the first case lacasse revealed higher activity in the monophasic region of the ternary phase diagram that corresponds to water-in-oil microemulsions, in These surfactantless systems have been mainly composed of non-polar solvents (as the "oil phase") with hexane [16,[121][122][123][125][126][127] and toluene [126,128,129] being the most frequently used. Tziala et al demonstrated for the first time the use of cyclic terpenes as natural organic solvents, such as α-pinene and D-limonene [130]. Such oils were efficiently used to formulate a stable surfactantless microemulsion where fungal chloroperoxidases and laccases retained their catalytic activity [131].…”

Section: Surfactantless Microemulsionsmentioning

confidence: 99%

“…This is because there are sufficient water molecules for adequately hydrating the enzyme. This behavior could also be attributed to the partition and therefore the availability of the lipophilic substrates in the enzyme aqueous microenvironment [130][131][132]. Nevertheless, in the case of cholesterol oxidase at the optimum water content, the entrapped enzyme showed lower stability in a temperature range of 25-40 • C in comparison to aqueous solutions [118,120].…”

Section: Surfactantless Microemulsionsmentioning

confidence: 99%

Oxidation Catalysis by Enzymes in Microemulsions

2017

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Microemulsions are regarded as "the ultimate enzyme microreactors" for liquid oxidations. Their structure, composed of water nanodroplets dispersed in a non-polar medium, provides several benefits for their use as media for enzymatic transformations. They have the ability to overcome the solubility limitations of hydrophobic substrates, enhance the enzymatic activity (superactivity phenomenon) and stability, while providing an interface for surface-active enzymes. Of particular interest is the use of such systems to study biotransformations catalyzed by oxidative enzymes. Nanodispersed biocatalytic media are perfect hosts for liquid oxidation reactions catalyzed by many enzymes such as heme peroxidases, phenoloxidases, cholesterol oxidase, and dehydrogenases. The system's composition and structural properties are important for better understanding of nanodispersion-biocatalyst interactions.

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“…[8] The solubility of substrates was improved by employing biphasic systems, [9] ionic liquids [10] or surfactant-free ternary water-organic solvent systems. [11] The inactivation of CPO can be partially suppressed by continuous [12] or slow controlled addition or by in-situ chemical [13] or electrochemical generation of H 2 O 2 . [14] However, slow addition can still produce local high concentrations of H 2 O 2 (hot spots) at the entry point.…”

Section: Introductionmentioning

confidence: 99%

Cross‐Linked Enzyme Aggregates of Chloroperoxidase: Synthesis, Optimization and Characterization

2009

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In this study we have optimized the conditions to precipitate and cross-link the enzyme chloroperoxidase (EC 1.11.1.10) from Caldariomyces fumago (CPO) using 1,2-dimethoxyethane as the precipitating agent. The coprecipitation of the enzyme with albumin and pentaethylenehexamine was needed for optimum results, presumably due to the low number of lysines available in CPO. The enzyme was immobilized with an activity recovery of 68%. The cross-linked enzyme aggregate showed higher temperature and pH stability, and better hydrogen peroxide tolerance than the free enzyme.

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Enhanced catalytic performance and stability of chloroperoxidase from Caldariomyces fumago in surfactant free ternary water–organic solvent systems

Cited by 36 publications

References 62 publications

Oxidative Halogenation with “Green” Oxidants: Oxygen and Hydrogen Peroxide

Oxidative Halogenation with “Green” Oxidants: Oxygen and Hydrogen Peroxide

Oxidation Catalysis by Enzymes in Microemulsions

Cross‐Linked Enzyme Aggregates of Chloroperoxidase: Synthesis, Optimization and Characterization

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