Recent biotechnological developments in the use of peroxidases

Colonna, Stefano; Gaggero, Nicoletta; Richelmi, C.; Pasta, Piero

doi:10.1016/s0167-7799(98)01288-8

Cited by 224 publications

(94 citation statements)

References 47 publications

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“…The high redox potential enables LIP to oxidize aromatic compounds with calculated ionization potential (IP) values of up to 9.0 eV (4). This has striking implications when considering the potential applications of peroxidases for useful biotransformations (5)(6)(7). LIP can be expected to oxidize a wider range of substrates and therefore have potential applications unsuitable for less potent peroxidases.…”

Section: Lignin Peroxidase (Lip)mentioning

confidence: 99%

Initial Steps of Ferulic Acid Polymerization by Lignin Peroxidase

Ward

Hadar²,

Bilkis

et al. 2001

Journal of Biological Chemistry

153

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The major products of the initial steps of ferulic acid polymerization by lignin peroxidase included three dehydrodimers resulting from ␤-5 and ␤-␤coupling and two trimers resulting from the addition of ferulic acid moieties to decarboxylated derivatives of ␤-O-4-and ␤-5-coupled dehydrodimers. This is the first time that trimers have been identified from peroxidase-catalyzed oxidation of ferulic acid, and their formation appears to be favored by decarboxylation of dehydrodimer intermediates. After initial oxidation, the coupling reactions appear to be determined by the chemistry of ferulic acid phenoxy radicals, regardless of the enzyme and of whether the reaction is performed in vitro or in vivo. This claim is supported by our finding that horseradish peroxidase provides a similar product profile. Lignin peroxidase (LIP)1 is considered to be one of the most important enzymes of the extracellular lignin degradation system secreted by the white rot fungus, Phanerochaete chrysosporium (1). Although LIP shares spectral and kinetic features with other peroxidases, the enzyme has several unique characteristics, including a redox potential higher than those of other peroxidases (2, 3). The high redox potential enables LIP to oxidize aromatic compounds with calculated ionization potential (IP) values of up to 9.0 eV (4). This has striking implications when considering the potential applications of peroxidases for useful biotransformations (5-7). LIP can be expected to oxidize a wider range of substrates and therefore have potential applications unsuitable for less potent peroxidases.Phenols are oxidized by peroxidases to generate phenoxy radicals, which couple with other substrate molecules to form dimeric, oligomeric, and polymeric products. This phenomenon can be exploited for the biocatalytic production of useful oligomers and polymers (6, 7), as well as for the treatment of wastewater streams polluted with toxic phenols (8 -10).Ferulic acid (FA), which is an extremely abundant and widespread cinnamic acid derivative (11), was chosen as a model substrate for studying the initial steps of LIP-catalyzed polymerization of phenolic compounds in vitro. In vivo, peroxidasecatalyzed oxidation of FA esterified to primary plant cell wall polysaccharides results in the formation of FA dehydrodimers, believed to enhance the rigidity and strength of the cell wall. A range of regio-isomeric dehydrodimers identified and quantified in several plant cell walls include products of ␤-␤Ј, ␤-5Ј, ␤-O-4Ј, 4-O-5Ј, and 5-5Ј radical coupling (12-15). Such dehydrodimers, along with FA, are also believed to act as nucleation sites in the lignification process, coupling with lignin monomers (16). This clearly indicates that FA dehydrodimers can be further oxidized. Indeed, certain dehydrodimers formed from oxidative coupling of FA have been reported to be more effective antioxidants than FA itself (17, 18). Their antioxidant activity appears to be related to the existence of a full conjugation system in the molecule. Nevertheless, the formati...

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Section: Lignin Peroxidase (Lip)mentioning

confidence: 99%

Initial Steps of Ferulic Acid Polymerization by Lignin Peroxidase

Ward

Hadar²,

Bilkis

et al. 2001

Journal of Biological Chemistry

153

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“…c) has catalytic ability in the enantioselective sulfoxidation of aryl alkyl sulfides to optically active sulfoxides, 24) which are of great pharmaceutical interest as chiral intermediates. 25) Moreover, immobilization of oxidative enzymes on MPSs enhances enzyme stability and increases ease of separation and recovery for reuse, while maintaining activity and selectivity. Ono et al, 26) described the immobilization of cyt.…”

Section: )12)mentioning

confidence: 99%

Preparation and catalytic evaluation of cytochrome c immobilized on mesoporous silica materials

Kato

Suzuki

Tanemura

et al. 2010

J. Ceram. Soc. Japan

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Cytochrome c (cyt. c, molecular size of 2.5 nm © 2.5 nm © 3.7 nm) was immobilized on six types of mesoporous silicates (MPS), having pore sizes from 2.8 to 15.0 nm, and their catalytic activities were evaluated by oxidation of thioanisol with H 2 O 2 . Among the silica materials, cyt. c immobilized on MPS pore size of 3.4 nm) showed the best catalytic activity, and its relative activity was improved 1.7 times over that of cyt. c solution. Enhancement of catalytic activity was obtained by immobilization on MPS having a similar size (mesopore) to the molecular size of cyt. c. Activity stability of cyt. c was also evaluated under the various conditions that caused protein inactivation, like HCl, urea, methanol, and guanidine. As results, stability was improved by the immobilization on silica material having a larger pore size (15.0 nm), offered an environment for encapsulating entire cyt. c molecules, inhibiting cyt. c from unfolding and irreversible decomposition.

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“…Several epoxide hydrolases (EHs) and Horse radish peroxidase (HRP) have recently been recognized as versatile biocatalysts in synthesis of enantiopure epoxides and their diols. They exhibit high enantioselectivity with broad substrate specificity and these enzymes do not require any cofactors in aqueous/buffer solution [7][8][9]. However, the use of biocatalysts in the industrial application is limited due to the difficulties associated with the enzyme stability and reuse.…”

Section: Introductionmentioning

confidence: 99%

A Green Approach towards the Synthesis of Enantio Pure Diols Using Horse Radish Peroxidase Enzyme Immobilized on Magnetic Nanoparticles

Deepthi¹,

Prasad²,

Reddy³

et al. 2014

GSC

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Enantiopure epoxides and their corresponding chiral vicinal diols serve as valuable intermediates in the synthesis of biologically active pharma and agro-compounds and also value added fine chemicals. Biocatalysts are well known for their selective hydrolysis of racemic epoxides to give optically pure chiral diols. This study highlights an efficient process of synthesis of chiral vicinal diols in good yields and enantioselectiviy using horse radish peroxidase enzyme immobilized on the amine functionalized magnetic nano particles (Fe 3 O 4 nanoparticles) as enzyme carriers. It also facilitates separation of MNP-immobilized enzymes by applying external magnetic field. The immobilization of magnetic nano particles was confirmed by transmission electron microscope (TEM) and scanning electron microscope (SEM). The MNP-immobilized peroxidase enzyme improved stability of the enzyme and has shown broader substrate specificity in enantioselective hydrolysis of racemic epoxides, under mild and environmentally friendly conditions. The methodology MNP-immobilized enzyme developed in the synthesis of chiral diols has a potential for use in large-scale applications.

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Recent biotechnological developments in the use of peroxidases

Cited by 224 publications

References 47 publications

Initial Steps of Ferulic Acid Polymerization by Lignin Peroxidase

Initial Steps of Ferulic Acid Polymerization by Lignin Peroxidase

Preparation and catalytic evaluation of cytochrome c immobilized on mesoporous silica materials

A Green Approach towards the Synthesis of Enantio Pure Diols Using Horse Radish Peroxidase Enzyme Immobilized on Magnetic Nanoparticles

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