Microorganisms for Sustainable Environment and Health
eBook - ePub

Microorganisms for Sustainable Environment and Health

  1. 534 pages
  2. English
  3. ePUB (mobile friendly)
  4. Available on iOS & Android
eBook - ePub

Microorganisms for Sustainable Environment and Health

About this book

Microorganisms for Sustainable Environment and Health covers hazardous pollutants released from natural as well as anthropogenic activities and implications on environmental and human health. This book serves as a valuable source of basic knowledge and recent developments in the clean technologies and pollution-associated diseases and abnormalities in the context of microorganisms. Focused on current solutions to various environmental problems in the field of bioremediation, it provides a detailed knowledge on the various types of toxic environmental pollutants discharged from different sources, their toxicological effects in environments, humans, animals and plants as well as their biodegradation and bioremediation approaches.This book helps environmental scientists and microbiologists learn about existing environmental problems and suggests ways to control or contain their effects by employing various treatment approaches.- Provides information on waste treatment approaches using microbes- Includes applications in biofuel and bioenergy production- Covers green belt development, hydroponics, phytoremediation, wetland treatment technology, and common effluent treatment plants (CETPs)- Discusses dissemination of antibiotic resistance among pathogenic microbes and strategies to combat multi-drug resistance (MDR)

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Yes, you can access Microorganisms for Sustainable Environment and Health by Pankaj Chowdhary,Abhay Raj,Digvijay Verma,Yusuf Akhter in PDF and/or ePUB format, as well as other popular books in Biological Sciences & Environmental Science. We have over one million books available in our catalogue for you to explore.
1

Recent advancement in the biotechnological application of lignin peroxidase and its future prospects

Pankaj Chowdhary1, Vishvas Hare1, Sujata Mani2, Anil Kumar Singh3,4, Surabhi Zainith1, Abhay Raj3 and Soumya Pandit5, 11Department of Microbiology, Babasaheb Bhimrao Ambedkar University (A Central University), Lucknow, India, 22Department of Biochemistry, Gramin Science (Vocational) College, Vishnupuri, Nanded, Maharashtra, India, 33Environmental Microbiology Laboratory, Environmental Toxicology Group, CSIR-Indian Institute of Toxicology Research (CSIR-IITR), Lucknow, India, 44Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India, 55Amity Institute of Biotechnology, Amity University, Mumbai, India

Abstract

The ligninolytic enzymes (laccase, manganese peroxidase, lignin peroxidase) have a wide range of applications, including in the industrial and environmental sectors. Lignin peroxidase (LiP; EC 1.11.1.14) is a heme-containing key enzyme of lignin degradation, and it is known as diaryl propane oxygenase. Being an oxidoreductase in chemical nature, LiP is an H2O2-dependent enzyme and catalyzes various phenolic and nonphenolic compounds. The diverse variety of microbes are known for LiP production in the environment. However, fungal-mediated ligninolytic enzymes have been studied extensively with its even greater advantages due to their thermostability, a wide range of pH values, fewer by-products, and high specificity. In the presenting chapter, we explore the ligninolytic enzymes, specially dedicated to lignin peroxidase. The broad and detailed information has dedicated to lignin peroxidases, like; the sources, production, mode of action, and various applications in industrial sectors. The potential use of this enzyme extends through many industries, including; pulp and paper, cosmetics, textile, bioremediation, energy, and cosmetics. Besides, this chapter also provides recent updates on lignin peroxidase production along with their current applications.

Keywords

Ligninolytic enzymes; lignin peroxidase; bioremediation; industrial application

1.1 Introduction

Microbes are ubiquitous and frequently present in very large numbers in environment. They are an integral part of the biological cycle, and are very essential for different substrate. Microbes on Earth can be either beneficial or harmful for humans, animals, and plants. Ligninolytic enzymes produced by microorganisms like bacteria, fungi, algae, etc. are of vital importance in the various industrial applications including pulp and paper manufacturing, textiles, and petrochemical industries (Munir et al., 2015; Chandra and Chowdhary, 2015; Chowdhary et al., 2019). White-rot fungi are well studied for producing four groups of enzymes, which play an important role in lignin degradation: laccase (EC 1.10.3.2), manganese peroxidase (MnP; EC 1.1.1.13), lignin peroxidase (LiP; EC 1.11.1.14), and versatile peroxidases (VP; EC 1.11.1.16). In recent literatures, LiP is known as ligninase. LiP was first isolated (in 1983) from the fungus Phanerochaete chrysosporium and it was found that it has the capability of oxidizing sites of mainly high redox potential, with moderately-activated aromatic rings of nonphenolic lignin compounds, which can comprise up to 90% of the polymer (β-o-4 linkage) (Aitken et al., 1994; Tien and Kirk, 1984). In addition, LiP is also responsible for oxidizing a variety of reducing substrates (Oyadomari et al., 2003). Besides this, LiP has been noted in a number of species of white-rot basidiomycetes and in actinomycetes (Pointing et al., 2005; Niladevi and Prema, 2005). It is well studied that peroxidases are heme-containing enzymes with catalytic cycles, which are involved in the activation of compound I and II intermediates by H2O2 and substrate reduction. Lignin peroxidase is an extracellular heme protein, reliant on hydrogen peroxide, with a low optimum pH and an unusually high redox potential (Erden et al., 2009; Piontek et al., 2001). LiPs have good potential for application in different types of process, because of their high redox potentials and their enlarged substrate range (Erden et al., 2009). LiPs have also catalyzed oxidative cleavage of C-C bonds and ether (C-O-C) bonds with high redox potential in nonphenolic aromatic substrates. However, in nature, potential lignin degraders secrete LiPs and its different isoforms. LiP isozymes are glycoproteins of 38–46 kDa (pI 3.2–4.0). The varieties of aromatic compounds are oxidized by LiP, therefore it has a role in the degradation of lignin and its derivatives (Baciocchi et al., 2001). LiP contains three tryptophans (Trp) and eight methionines (Met). Amino acid tyrosine (Tyr) is absent in LiP and it also doesn’t contain free cysteine (Cys). The highest carbohydrate level containing isozyme was most sensitive to changes in environmental factors. The demand for various ligninolytic enzymes complexes of white-rot fungi in industry and biotechnology is always growing due to their use in different techniques (Chowdhary et al., 2018). LiP has little substrate specificity, reacting with a huge form of lignin model compounds or even unrelated molecules (Barr and Aust, 1994). It has the distinction of being able to oxidize methoxylated fragrant rings without an unfastened phenolic group, producing cation radicals that may react further by a raft of pathways which includes ring-opening, demethylation, and phenol dimerization (Haglund, 1999). To degrade high redox potential compounds laccases require mediators but LiP needs H2O2 to initiate the catalysis reaction. In both fungi and bacteria, LiP has been reported to be a ligninolytic enzyme and mineralizes 3- and 4-ring polycyclic aromatic hydrocarbons (PAHs) and also various types of recalcitrant compounds, polychlorinated biphenyl, chlorophenols, and synthetic dyes (Wesenberg et al., 2003; Antonopoulos et al., 2001). Lignin peroxidase also shows the highest bioelectrocatalytic activity at atomic resolution and this makes it available for the commercial development of biosensors for polymeric phenol or lignin (Christenson et al., 2004). The above research data shows that the LiP has high suitability for pot...

Table of contents

  1. Cover image
  2. Title page
  3. Table of Contents
  4. Copyright
  5. List of Contributors
  6. About the editors
  7. Preface
  8. 1. Recent advancement in the biotechnological application of lignin peroxidase and its future prospects
  9. 2. Microbes mediated approaches for environmental waste management
  10. 3. Actinobacteria for the effective removal of toxic dyes
  11. 4. Arsenic toxicity: adverse effect and recent advance in microbes mediated bioremediation
  12. 5. Recent advances in the application of biofilm in bioremediation of industrial wastewater and organic pollutants
  13. 6. Waste treatment approaches for environmental sustainability
  14. 7. Biodegradation of environmental pollutant through pathways engineering and genetically modified organisms approaches
  15. 8. Exploring the microbiome of smokeless tobacco
  16. 9. Microbial ligninolytic enzymes and their role in bioremediation
  17. 10. Recent advancements in microalgal-induced remediation of wastewaters
  18. 11. Cyanobacteria as source of novel antimicrobials: a boon to mankind
  19. 12. Composite nanostructure: a potential material for environmental safety and health
  20. 13. In silico bioremediation strategies for removal of environmental pollutants released from paper mills using bacterial ligninolytic enzymes
  21. 14. Pectinases: from microbes to industries
  22. 15. Understanding and combating the antibiotic resistance crisis
  23. 16. Multidrug resistance in pathogenic microorganisms
  24. 17. Microbial hydrogen production: fundamentals to application
  25. 18. Antibiotics: mechanisms of action and modern challenges
  26. 19. Food poisoning hazards and their consequences over food safety
  27. 20. Application of microbial consortia in degradation and detoxification of industrial pollutants
  28. 21. Environmental pollution: causes, effects, and the remedies
  29. 22. Microplastic degradation by bacteria in aquatic ecosystem
  30. 23. The role of microbial pathogens in cancer development: a potential guide to anticancer drugs
  31. Index