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Role of Genomics, Metagenomics, and Other Meta-Omics Approaches for Expunging the Environmental Contaminants by Bioremediation
Published in Vineet Kumar, Vinod Kumar Garg, Sunil Kumar, Jayanta Kumar Biswas, Omics for Environmental Engineering and Microbiology Systems, 2023
Atif Khurshid Wani, Daljeet Singh Dhanjal, Nahid Akhtar, Chirag Chopra, Abhineet Goyal, Reena Singh
Peroxidases are a diverse group of ubiquitous enzymes that mediate lignin oxidation by utilizing H2O2 (hydrogen peroxide). These peroxidases have been grouped based on the heme group’s presence or absence (Pande et al., 2019). Group I consists of intracellular peroxidases that include ascorbate peroxidase, cytochrome peroxidase, and catalase peroxidases. Group II is a category of secretory biosynthetic fungal enzymes that include manganese peroxidase and lignin peroxidase from Coprinus cinereus and Phanerochaete chrysosporium. Group II peroxidases are well known for degrading wood lignin (Darwesh et al., 2019). Peroxidases are produced from different sources, including animals, plants, and microbes. Microbial sources of peroxidases include Bacillus subtilis, Candida krusei, Bacillus sphaericus, P. chrysosporium, and Thermobifida fusca. Several microbial peroxidases have been used to degrade the xenobiotic dyes, which are commonly challenging to degrade (Bansal and Kanwar, 2013; Zainith et al., 2020). The removal of acid orange (azo dye) and chromate by Brevibacterium casei have been studied in detail. Pleurotus ostreatus, known for the production of an extracellular peroxidase, has been reported as having decolourization properties against Remazol blue and other groups such as polymeric dyes, heterocyclic azo dyes, and triarylmethane (Bansal and Kanwar, 2013).
Biodegradation and Biocatalysis Aspects of Direct Bioethanol Production by Fungi in a Single Step Named Consolidated Bioprocessing
Published in Ayerim Y. Hernández Almanza, Nagamani Balagurusamy, Héctor Ruiz Leza, Cristóbal N. Aguilar, Bioethanol, 2023
Luis Fernando Amador Castro, Danay Carrillo Nieves
Peroxidases are widely distributed among plants, animals, and microorganisms. These enzymes catalyze the oxidation of different substrates, using H2O2 or other peroxides as electron acceptors [35]. Most of the peroxidases are heme enzymes that contain an iron protoporphyrin IX prosthetic group, although there are many nonheme peroxidases [36]. Heme peroxidases can be mainly classified into two superfamilies animal and non-animal (plant) peroxidases [37, 38]. Non-animal peroxidases are further subdivided into three classes. Class I are intracellular peroxidases that have been found in bacteria, fungi, plants, and some protists, examples include cytochrome c, catalase, and ascorbate peroxidases. Class II refers to extracellular fungal peroxidases in which lignin, manganese, and versatile peroxidases (VPs) are included. Class III are secreted peroxidases only found in plants [39]. Animal peroxidases have also been subclassified as in the case of plant peroxidases, however, its subclassification is more complex [37]. Some heme peroxidases such as DyPs do not fit within the previously mentioned superfamily classification and constitute its family [40]. Different peroxidase phylogenetic classifications have also been proposed [41, 42].
Microbial Strategies for the Decolorization and Degradation of Distillery Spent Wash Containing Melanoidins
Published in M.H. Fulekar, Bhawana Pathak, Bioremediation Technology, 2020
The current trend for environmental pollution control is biodegradation processes with the help of various microorganisms. Every pollutant required specific enzymes to degrade or alter its configuration and convert the pollutant into nonhazardous waste. Melanoidins could also be decolorized and degraded by several enzymes, for example, peroxidases, oxidoreductases, cellulolytic enzymes, cyanidase, proteases and amylases (Santal and Singh, 2013). Among them significant ligninolytic enzymes are manganese peroxidase (MnP), lignin peroxidase (LiP) and laccase, reported by many authors for the degradation and detoxification of melanoidins (Sangeeta et al., 2011; Sangeeta and Chandra, 2012; Sangeeta and Chandra, 2013). Those enzymes have been reported for the decolorization and degradation of many recalcitrant compounds, as well as dyes. They also included as oxidoreductases two categories of peroxidases, e.g. lignin peroxidase and manganese peroxidase.
Global mapping of research outputs on nanoparticles with peroxidase mimetic activity from 2010–2019
Published in Inorganic and Nano-Metal Chemistry, 2023
Raphael Idowu Adeoye, Kunle Okaiyeto, Oluwafemi Omoniyi Oguntibeju
Peroxidase utilizes peroxide to oxidize various organic molecules (RH) to radicals (R•) in two sequential one-electron steps with concomitant reduction of peroxide.[1] Peroxidases have gained wide applications in bioremediation, biocatalysis, diagnosis, biosensors, protein engineering, food technology, biotechnology, and therapeutics.[2–4] Natural peroxidases are prone to suicide inactivation by their substrate.[5] In addition, they are unstable and are easily denatured in harsh environmental conditions, and are expensive to isolate and purify.[6] These drawbacks have limited their applications in all essential processes and have spurred scientists to explore artificial enzymes with peroxidase activity as alternatives to natural peroxidases. In recent years, artificial enzymes with peroxidase mimetic activity like DNA-hemin complexes,[2] nanozymes,[7] cyclo-dextrin,[8] chitosan[9] and Schiff bases have been explored.
Modelling and analysis of haemoglobin catalytic reaction kinetic system
Published in Mathematical and Computer Modelling of Dynamical Systems, 2020
Yanhong Liu, Hui Lv, Bin Wang, Deyun Yang, Qiang Zhang
Because of the high activity of peroxidase, it is often used for the determination of hydrogen peroxide (H2O2) and glucose [1,2]. However, peroxidase has disadvantages because of its limited availability, high price, harsh reaction conditions, and rapid degeneration and inactivation, which limit its application range. Therefore, it is important to identify possible substitutes [3,4]. Haemoglobin (Hb) is a respiratory protein found in the erythrocytes of vertebrates [5–7], which plays important roles in oxygen transport and energy metabolism, such as oxygen transmission, the decomposition of H2O2 and the transfer of electrons [8]. Wang et al. [9] experimentally studied the catalytic properties of Hb peroxidase. The results show that Hb has good catalytic activity of peroxidase. Based on this, to further study the characteristics of Hb peroxidase, a mathematical model of an Hb reaction is established, which can help engineers and scientists understand the activity of Hb peroxidase and better exploit it in industrial production and life.
Antioxidant response mechanism of freshwater microalgae species to reactive oxygen species production: a mini review
Published in Chemistry and Ecology, 2020
Adamu Yunusa Ugya, Tijjani Sabiu Imam, Anfeng Li, Jincai Ma, Xiuyi Hua
Catalase and Peroxidase are tetrameric and heme-containing antioxidant enzymes produced by freshwater microalgae to reduce hydrogen peroxide and more active hydroperoxide such as lipid peroxide equation (5).The production site for catalase in freshwater microalgae is peroxisome although several studies including Mhamdi et al. [127] show that catalase can be produced in the chloroplast, cytosol, and mitochondria. The three known groups of catalases are two heme-containing catalases (monofunctional and bifunctional) and one non-heme containing catalases [128]. Both monofunctional and bifunctional heme-containing catalases are sensitive to cyanide although they are both different in sequences, structures and action mechanisms [129]. The two types of peroxidase are ascorbate peroxidase and glutathione peroxidase. Ascorbate peroxidase is regarded as a heme-containing peroxide that plays an important role in H2O2 conversion by freshwater microalgae. Although, scanty or no literature on isozyme of ascorbate peroxidase has been reported these enzymes used ascorbate as a specific electron donor [130]. Glutathione peroxidase plays a vital role in the reduction of H2O2 by oxidation of glutathione, the oxidised glutathione is then reduced by glutathione reductase as a result of electron derived from NADPH.