Horseradish Peroxidase: Structure, Functions and Applications

Maarten Uzun (Editor)

Series: Biochemistry Research Trends
BISAC: SCI007000

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In this compilation, the authors discuss the commercial source for the enzyme horseradish peroxidase, the tuberous roots of the horseradish plant which is native to the temperate regions of the world. Horseradish peroxidase is an oxidoreductase belonging to the highly ubiquitous group of peroxidases, indicating that this enzyme came into existence in the early stages of evolution and has been conserved thereafter.

Following this, the authors discuss the latest advancements and innovations in the field of enzymatic electrochemical sensors based on the electrical communication between horseradish peroxidase and the enzyme’s modified electrodes surfaces.

In conclusion, the authors discuss the potential for horseradish peroxidase use in colored wastewater treatment. C. I. Acid Violet 109 was used as a model dye in order to examine the feasibility of horseradish peroxidase application in the removal of anthraquinone class of synthetic dyes. The reaction conditions were optimized in terms of dye, enzyme and H2O2 concentration as well as temperature and pH influence.
(Imprint: Nova)

Preface

Chapter 1. Horseradish Peroxidase: At the Tip of the Iceberg
(Mugdha Ambatkar and Usha Mukundan, Plant Biotechnology Research Laboratory, Ramniranjan Jhushtranjhunwala College, Mumbai, India)

Chapter 2. Electrical Communication between “Horseradish Peroxidase” and Modified Electrodes with Nanomaterials: Application as Enzymatic Electrochemical Biosensors
(Lenys Fernández, Augusto Rodríguez, Gema González, Rafael Úribe, Antonio Díaz and Patricio Espinoza-Montero, Escuela de Ciencias Químicas, Pontificia Universidad Católica del Ecuador Quito, Ecuador)

Chapter 3. Removal of Synthetic Dyes from Wastewaters Using Horseradish Peroxidase
(Nataša Ž. Šekuljica, Nevena Ž. Prlainović, Zorica D. Knežević-Jugović and Dušan Ž. Mijin, Innovation Center Faculty of Technology and Metallurgy, Belgrade, Serbia, and others)

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