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Sunday, April 19, 2020 | History

2 edition of Biocatalysis based on heme peroxidases found in the catalog.

Biocatalysis based on heme peroxidases

Eduardo DГ­az Torres

Biocatalysis based on heme peroxidases

peroxidases as potential industrial biocatalysts

by Eduardo DГ­az Torres

  • 278 Want to read
  • 7 Currently reading

Published by Springer-Verlag in New York .
Written in English

    Subjects:
  • Enzymes,
  • Peroxidase,
  • Industrial applications

  • Edition Notes

    Includes bibliographical references and index.

    StatementEduardo Torres, Marcela Ayala, editors
    Classifications
    LC ClassificationsTP248.E5 B55 2010
    The Physical Object
    Paginationxi, 358 p. :
    Number of Pages358
    ID Numbers
    Open LibraryOL25101289M
    ISBN 10364212626X
    ISBN 109783642126260
    LC Control Number2010932759
    OCLC/WorldCa646113711


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Biocatalysis based on heme peroxidases by Eduardo DГ­az Torres Download PDF EPUB FB2

The book Heme per- idases covers discussion on three-dimensional structure, reaction mechanism, kinetics, and spectral properties of representative enzymes from bacterial, plant, fungal, and animal origin. Sincevast information on basic but also applied aspects of heme peroxidases has been cturer: Springer.

This monograph describes many applications of peroxidase-based biocatalysis in the biotechnology industry. The need for such a book emerges from the considerable amount of new data regarding the phylogeny, reaction mechanisms, thermodynamic characterization and structural features of fungal and plant heme peroxidases that has been generated in the past 10 years, since the last specialized book.

The book Heme per- idases covers discussion on three-dimensional structure, reaction mechanism, kinetics, and spectral properties Biocatalysis based on heme peroxidases book representative enzymes from Biocatalysis Based on Heme Peroxidases - Biocatalysis based on heme peroxidases book as Potential Industrial Biocatalysts | Eduardo Torres | Springer.

Biocatalysis Based On Heme Peroxidases. Home; fundamental understanding The behavior of; About The The book does not include an exhaustive listing of references but rather a selected collection to enrich discussion and to allow envisioning future directions for research.

The book Heme per- idases covers discussion on three-dimensional structure. The book Heme per- idases covers discussion on three-dimensional structure, reaction mechanism, kinetics, and spectral properties of representative enzymes from bacterial, plant, fungal, and animal origin.

Sincevast information on basic but also applied aspects of heme peroxidases has been : Springer Berlin Heidelberg. from book Biocatalysis Based on Heme Peroxidases (pp) Biocatalysis Based on Heme Peroxidases.

Chapter June This book presents recent advances on evolution, structure-function relation and catalytic mechanism as well as applied aspects such as bioreactor and protein engineering. It will help in the design of enhanced biocatalysts and biocatalytic processes.

The last systematic description of heme peroxidases was published in by Brian Dunford, from the University of Alberta in Canada. Oxidation is a central transformation reaction in synthetic chemistry. For decades, oxidation reactions were carried out with stoichiometric toxic reagents such as chromates.

For the past few decades, biocatalysis with heme peroxidases and peroxygenases have emerged as an additional pillar for environmentally benign oxidation : Marcela Ayala, Eduardo Torres. The last systematic description of heme peroxidases was published in by Brian Dunford, from the University of Alberta in Canada.

The book Heme per- idases covers discussion on three-dimensional structure, reaction mechanism, kinetics, and spectral properties of representative enzymes from bacterial, plant, fungal, and animal : Hardcover. AbstractIn recent years, the continuous and accumulative discharge of toxic.

Request PDF | Biocatalysis Based on Heme Peroxidases | This monograph describes many applications of peroxidase-based biocatalysis in the biotechnology industry. The need for such a book. Not Available adshelp[at] The ADS is operated by the Smithsonian Astrophysical Observatory under NASA Cooperative Agreement NNX16AC86ACited by: Four subfamilies of dyp-type peroxidases capable of degradation of various xenobiotics are abundant mainly among bacteria E.

Torres and M. Ayala (eds.), Biocatalysis Based on Heme Peroxidases, 7 DOI /_2, # Springer-Verlag Berlin Heidelberg 8 M. Za´mocky´ and C. Obinger and fungi. The book Heme per- idases covers discussion on three-dimensional structure, reaction mechanism, kinetics, and spectral properties of representative enzymes from bacterial, plant, fungal, and animal origin.

Sincevast information on basic but also applied aspects of heme peroxidases has been generated. Biocatalysis based on heme peroxidases | Eduardo Torres - This monograph describes many applications of peroxidase-based biocatalysis in the biotechnology industry.

The need for such a book emerges from the considerable amount of new data regarding the phylogeny, reaction mechanisms, thermodynamic.

Biocatalysis Based on Heme Peroxidases, ISBN Springer-Verlag Berlin Heidelberg,p. : Abstract 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.

This chapter. Abstract 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.

Biocatalysis Based on Heme Peroxidases. Biocatalysis Based on Heme Peroxidases pp () Molecular Phylogeny of Heme Peroxidases. In: Torres E., Ayala M. (eds) Biocatalysis Based on Heme Peroxidases. Springer, Berlin, Heidelberg. Buy this book on publisher's site; Reprints and Permissions; Personalised by: Redox Biocatalysis begins with a discussion of the biochemical features of redox enzymes as well as cofactors and cofactor regeneration methods.

Next, the authors present a variety of topics and materials to the research and development of full-scale industrial applications, including. Heme peroxidases. This book reflects the tremendous growth peroxidases research has experienced in recent years, providing for the first time in over three decades a systematic, up-to-date.

Environmental protection is, doubtless, one of the most important challenges for the human kind. The huge amount of pollutants derived from industrial activities represents a threat for the environment and ecologic equilibrium.

Phenols and halogenated phenols, polycyclic aromatic hydrocarbons, endocrine disruptive chemicals, pesticides, dioxins, polychlorinated biphenyls, industrial dyes, and.

Heme peroxidases, catalases, and other peroxidases such as vanadium and selenium peroxidase Relevant plant and animal physiology This one-stop reference is a vital reference for biochemists, biologists, biochemical engineers, physiologists, environmental and pharmaceutical researchers, and others interested in the study and use of peroxidases Cited by: Applications and prospective of peroxidase biocatalysis in the environmental field (Cristina Torres-Duarte and Rafael Vazquez-Duhalt) CHALLENGES IN THE APPLICATION OF PEROXIDASES Enzyme technology of peroxidases: immobilization, chemical and genetic modification (Adriana Longoria, Raunel Tinoco and Eduardo Torres).

In Biocatalysis Based on Heme Peroxidases (Torres E.,Ayala M., Eds.), Springer Berlin Heidelberg (). CRC handbook of chemistry and physics:a ready-reference book of chemical and physical data, CRC, BocaRaton, Fla, [32] Waterhouse A.L., Determination of total phenolics. In CurrentProtocols in Food Analytical Chemistry, John Wiley.

Torres, Ayala M (Eds.), In Biocatalysis Based on Heme Peroxidases — Peroxidases as Potential Industrial Biocatalysts, vol 1, Springer-Verlag (), pp. Google Scholar 52Cited by: Introduction. The peroxidase-catalase superfamily (named according to the two main enzymatic activities, see below), also known as the non-animal superfamily or the superfamily of bacterial, fungal and plant heme peroxidases, is very likely the most abundant evolutionary line of heme peroxidases in both prokaryotic and eukaryotic tly about protein sequences match the criteria Cited by: The last systematic description of heme peroxidases was published in by Brian Dunford, from the University of Alberta in Canada.

The book Heme per- idases covers discussion on three-dimensional structure, reaction mechanism, kinetics, and spectral properties of representative enzymes from bacterial, plant, fungal, and animal origin.

Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme: Fe 3+ + H 2 O 2 ⇌ [Fe 4+ =O]R' (Compound I) + H 2 O [Fe 4+ =O]R' + substrate --> [Fe 4+ =O]R (Compound II) + oxidized substrate [Fe 4+ =O]R + substrate --> Fe 3+ + H 2 O + oxidized InterPro: IPR Biocatalysis based on heme peroxidases.

Springer, Berlin. str. BRENDA: BRENDA entry. In general, hydrogen peroxide is a stable and relatively mild oxidant and it can be regarded as the ultimate “green” reagent because water and oxygen are the only by-products. Besides the direct application of H2O2 in chemical processes more and more enzymatic syntheses based on hydrogen peroxide were develoCited by: 8.

An up-to-date overview of diverse findings and accomplishments in biocatalysis and bioenergy With the high price of petroleum and researchers worldwide seeking new means of producing energy, this comprehensive book on biocatalysis for bioenergy and biofuel applications is very timely.

Following an inspiration from the fine structure of natural peroxidases, such as horseradish peroxidase (HRP), an artificial peroxidase was constructed through the self-assembly of diblock copolymers and hemin, which formed a functional micelle with peroxidase-like by: 1.

Introduction. The peroxidase–catalase superfamily (named according to the two main enzymatic activities), also known as the non-animal superfamily or the superfamily of bacterial, fungal and plant heme peroxidases, is very likely the most abundant line of heme peroxidases in both prokaryotic and eukaryotic first classification of this superfamily presented by K.G.

Welinder in Cited by: Ortiz de Montellano PR () Catalytic mechanisms of heme peroxidases. In: Torres E, Ayala M (eds) Biocatalysis based on heme peroxidases−peroxidases as potential industrial biocatalysts, 1st edn. Springer-Verlag, Berlin, pp 80– Google ScholarCited by: Official website of [Peroxidases as biocatalysts].

Novel and more robust fungal peroxidases as industrial biocatalysts. Novel and more robust fungal peroxidases as industrial biocatalysts.

This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under. All heme-proteins, including peroxidases, are inactivated in the presence of some concentrations of hydrogen peroxide.

This process, described as a suicide inactivation, is especially important in the absence of reducing substrates, but its mechanism has not been yet fully elucidated [ 18 ].Cited by: Heme proteins with histidine as proximal ligand.

The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3′,5,5′-tetramethylbenzidine (TMB) and 2,2′-azinobis(3-ethylbenzthiazolinesulfonic acid) (ABTS).

Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate. Biocatalysis based on heme peroxidases. Springer, Berlin. стр. 7— Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book BRENDA: BRENDA pristup.

heme; Comments: Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) (ABTS).

Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and. Heme peroxidases, catalases, and other peroxidases such as vanadium and selenium peroxidase Relevant plant and animal physiology This one-stop reference is a vital reference for biochemists, biologists, biochemical engineers, physiologists, environmental and pharmaceutical researchers, and others interested in the study and use of peroxidases.

In this work, a commercial peroxidase was immobilized onto porous silicon (PS) support functionalized with 3-aminopropyldiethoxysilane (APDES) and the performance of the obtained catalytic microreactor was studied.

The immobilization steps were monitored and the activity of the immobilized enzyme in the PS pores was spectrophotometrically by:   The first Dyp-type protein was isolated in from Thanatephorus cucumeris Dec 1 (formerly Geotrichum candidum Dec 1, DyP Dec 1), a dye-decolorizing fungus [].The enzyme is a glycoprotein with low homology to all other known peroxidases.

It has novel activity on anthraquinone dyes with low pH optimum (–) [12, 13].More DyPs have been later found in by: 2.Biocatalysis Based on Heme Peroxidases: Peroxidase Marcela Ayala.

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