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An overview of enzyme technology applied to peroxidases is made. Immobilization on organic, inorganic, and hybrid supports; chemical modification of amino acids and heme group; and genetic modification by site-directed and random mutagenesis are included. Different strategies that were carried out to improve peroxidase performance in terms of stability, selectivity, and catalytic activity are analyzed...
In this chapter, the engineering aspects of processes catalyzed by peroxidases will be presented. In particular, a discussion of the existing technologies that utilize peroxidases for different purposes, such as the removal of recalcitrant compounds or the synthesis of polymers, is analyzed. In the first section, the essential variables controlling the process will be investigated, not only those...
Peroxidases use H2O2 as electron acceptor in order to catalyze a variety of oxidative reactions through a catalytic cycle with two intermediates. Additionally to these intermediates, a third species (Compound III) is produced when ferric peroxidases are exposed to an excess of H2O2. Compound III is a peroxy-FeIII− porphyrin free radical, the best described of the intermediates leading to the irreversible...
The industrial importance of peroxidases has led to much research in the past two decades on the development of a cost effective and efficient production process for peroxidases. Unfortunately, even today, no clear answers can be given to questions such as (1) should the peroxidase be expressed in bacteria, yeast, or fungi? (2) which is the optimal production strain (e.g., protease deficient, heme...
World population is expected to increase from 6.5 billion in 2005 to 8.3 billion by 2030. Simultaneously, the average per capita income could rise from USD 5,900 in 2005 to USD 8,600, a 46% increase. A larger population with increased acquisitive power, along with the challenge of developing environmentally sustainable processes will be the driving force for the emergence of bioeconomy. According...
All currently available gene sequences of heme peroxidases can be phylogenetically divided in two superfamilies and three families. In this chapter, the phylogenetics and genomic distribution of each group are presented. Within the peroxidase–cyclooxygenase superfamily, the main evolutionary direction developed peroxidatic heme proteins involved in the innate immune defense system and in biosynthesis...
This chapter begins with a description of the main structural features of heme peroxidases representative of the two large superfamilies of plant–fungal–bacterial and animal peroxidases, and the four additional (super)families described to date. Then, we focus on several fungal peroxidases of high biotechnological potential as industrial biocatalysts. These include (1) ligninolytic peroxidases from...
Redox potential of peroxidases greatly influences the range of oxidizable substrates: in principle, peroxidases may only catalyze the oxidation of substrates with lower redox potential. There is substantial information on the factors that modulate the redox potential of heme proteins. Both theoretical and experimental evidence highlight the most significant contributions arising from the interaction...
The hemoprotein peroxidases produce a reactive intermediate, Compound I, whose reactions are controlled by the protein environment. In conventional peroxidases with a histidine iron ligand, access to the Compound I ferryl species is restricted by the protein, favoring the transfer of single electrons from the substrate to an exposed heme edge. If the protein has a suitably placed oxidizable residue...
All currently available gene sequences of heme peroxidases can be phylogenetically divided in two superfamilies and three families. In this chapter, the phylogenetics and genomic distribution of each group are presented. Within the peroxidase–cyclooxygenase superfamily, the main evolutionary direction developed peroxidatic heme proteins involved in the innate immune defense system and in biosynthesis...
This chapter begins with a description of the main structural features of heme peroxidases representative of the two large superfamilies of plant–fungal–bacterial and animal peroxidases, and the four additional (super)families described to date. Then, we focus on several fungal peroxidases of high biotechnological potential as industrial biocatalysts. These include (1) ligninolytic peroxidases from...
Redox potential of peroxidases greatly influences the range of oxidizable substrates: in principle, peroxidases may only catalyze the oxidation of substrates with lower redox potential. There is substantial information on the factors that modulate the redox potential of heme proteins. Both theoretical and experimental evidence highlight the most significant contributions arising from the interaction...
The hemoprotein peroxidases produce a reactive intermediate, Compound I, whose reactions are controlled by the protein environment. In conventional peroxidases with a histidine iron ligand, access to the Compound I ferryl species is restricted by the protein, favoring the transfer of single electrons from the substrate to an exposed heme edge. If the protein has a suitably placed oxidizable residue...
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