Biotechnological applications of peroxidases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-01

AUTHORS

Carlos Regalado, Blanca E. García-Almendárez, Miguel A. Duarte-Vázquez

ABSTRACT

Peroxidases are widely distributed in nature. Reduction of peroxides at the expense of electron donating substrates, make peroxidases useful in a number of biotechnological applications. Enzymes such as lignin peroxidase and manganese peroxidase, both associated with lignin degradation, may be successfully used for biopulping and biobleaching in the paper industry, and can produce oxidative breakdown of synthetic azo dyes. Oxidative polymerization of phenols and aromatic amines conducted by horseradish peroxidase (HRP) in water and water-miscible organic solvents, may lead to new types of aromatic polymers. Site directed mutagenesis of HRP has been used to improve the enantioselectivity of arylmethylsulfide oxidations. Peroxidase has a potential for soil detoxification, while HRP as well as soybean and turnip peroxidases have been applied for the bioremediation of wastewater contaminated with phenols, cresols, and chlorinated phenols. Peroxidase based biosensors have found use in analytical systems for determination of hydrogen peroxide and organic hydroperoxides, while co-immobilized with a hydrogen peroxide producing enzyme, they can be used for determination of glucose, alcohols, glutamate and choline. Peroxidase has also been used for practical analytical applications in diagnostic kits, such as quantitation of uric acid, glucose, cholesterol, lactose, and so on. Enzyme linked immunorbent assay (ELISA) tests on which peroxidase is probably the most common enzyme used for labeling an antibody, are a simple and reliable way of detecting toxins, pathogens, cancer risk in bladder and prostate, and many other analytes. Directed evolution methods, appear to be a valuable alternative to engineer new catalyst forms of plant peroxidases from different sources to overcome problems of stability and to increase thermal resistance. More... »

PAGES

243-256

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/b:phyt.0000047797.81958.69

DOI

http://dx.doi.org/10.1023/b:phyt.0000047797.81958.69

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1008343434


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387 schema:name Departamento de Investigación y Posgrado en Alimentos, PROPAC, Facultad de Química, Universidad Autónoma de Querétaro, 76010, Querétaro, Mexico
388 Facultad de Ciencias Naturales, Universidad Autónoma de Querétaro, Mexico
389 rdf:type schema:Organization
 




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