Peroxidases, one of the key antioxidant enzymes, are widely distributed in nature and catalyze oxidation of various electron donor substrates concomitant with the decomposition of H 2 O 2. The non-animal plant peroxidases (class III peroxidase) are involved in various essential physiological processes of plant growth and development throughout their life cycle. In view of the capability of peroxidases to catalyze the redox reaction for a wide range of substrates, they are considered as one of the important enzyme from the point of view of their various medicinal, biochemical, immunological, biotechnological and industrial applications. They have been successfully used for biopulping and biobleaching in the paper and textile industries. Peroxidases have also been used in organic synthesis, bioremediation, as well as various analytical applications in diagnostic kits, ELISA. Peroxidase based biosensors find application in analytical systems for determination of hydrogen peroxide, glucose, alcohols, glutamate, and choline etc. Thus, in view of array of physiological functions as well as industrial applications, the peroxidases have conquered a dominant position in research groups and become one of the most extensively studied enzymes. In this direction, the present review embodies the classification, mechanism of action, major physiological functions as well as industrial applications of plant peroxidases.
Syphilis, a slow progressive and the third most common sexually transmitted disease found worldwide, is caused by a spirochete gram negative bacteria Treponema pallidum. Emergence of antibiotic resistant T. pallidum has led to a search for novel drugs and their targets. Subtractive genomics analyses of pathogen T. pallidum and host Homo sapiens resulted in identification of 126 proteins essential for survival and viability of the pathogen. Metabolic pathway analyses of these essential proteins led to discovery of nineteen proteins distributed among six metabolic pathways unique to T. pallidum. One hundred plant-derived terpenoids, as potential therapeutic molecules against T. pallidum, were screened for their drug likeness and ADMET (absorption, distribution, metabolism, and toxicity) properties. Subsequently the resulting nine terpenoids were docked with five unique T. pallidum targets through molecular modeling approaches. Out of five targets analyzed, D-alanine:D-alanine ligase was found to be the most promising target, while terpenoid salvicine was the most potent inhibitor. A comparison of the inhibitory potential of the best docked readily available natural compound, namely pomiferin (flavonoid) with that of the best docked terpenoid salvicine, revealed that salvicine was a more potent inhibitor than that of pomiferin. To the best of our knowledge, this is the first report of a terpenoid as a potential therapeutic molecule against T. pallidum with D-alanine:D-alanine ligase as a novel target. Further studies are warranted to evaluate and explore the potential clinical ramifications of these findings in relation to syphilis that has public health importance worldwide.
SynopsisPoly(buty1 methacrylate) (PBMA) was grafted onto wool in the presence of air and nitrogen atmosphere using potassium bromate and thioaceticacid (TAA) as redox initiating system, under different reaction conditions. The percentage grafting and percentage efficiency have been determined as a function of various reaction variables and the results have been compared. The graftcopolymer was characterized by scanning electron micrograph, thermogravimetry, and molecular weight.
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