The Role Of Peroxidases Within Green Chemistry Transformations

Abstract

Peroxidases are oxidoreductase enzymes that have become economically important in newlinecoal, paper, medicines, dyes, chemicals, and nanotechnology industries. In recent years, they newlinehave widely gained attention as biocatalysts for their robust catalytic activity, specificity, and newlineregioselective functionality. They are utilized to oxidize a wide variety of organic and inorganic newlinesubstrates in the presence of hydrogen peroxides or organic peroxides. Chapter 1 overviews newlinedifferent peroxidases, their historical background, sources, physiochemical characteristics, and newlinecatalytic mechanisms. The review section explores the potential applications of peroxidases in newlinethe remediation of phenols and their derivatives, pharmaceuticals and personal care products, newlinedyes, agrochemicals, and petrochemicals. Other applications in biotechnology for fabricating newlineperoxidase-based biosensors and the recent trend in nanotechnology are also reviewed in detail. newlineThe analytical and instrumentation techniques used for the isolation, purification, and newlinecharacterization of luffa peroxidase (LPrx) are presented in Chapter 2. There are detailed newlinedescriptions of the steps and methods followed for enzyme dialysis, ion exchange newlinechromatography, SDS-PAGE, MALDI TOF MS, kinetic studies, inhibition studies, newlinephytotoxicity assessment of phenolic compounds, and biotransformation. The bioinformatics newlinestudy of LPrx includes in silico analysis using the latest software, techniques, and protocols. newlineChapter 3 covers the physiochemical characteristics of luffa peroxidase (LPrx) from newlineLuffa acutangula, and appropriate tables and charts were used to enhance the presentation of newlinethe findings and the results. Isolation and purification of LPrx involved extraction, newlineconcentration with ammonium sulfate precipitation, dialysis, and ion exchange newlinechromatography. The novel peroxidase, LPrx was purified to 10-fold with a recovery newlinepercentage of 20.93. A single band was observed in both native and SDS-PAGE gel after electrophoresis confirmed the purity and the homogeneity of LPrx. The hemoc