Microorganisms for Sustainable Environment and Health

mechanisms.

Preface

Microorganisms for Sustainable Environment and Health covers the potential role of microbial biotechnology for the betterment of our daily lifestyle. This book covers the various applications of microbes for environmental sustainability. There are various useful microbes, which may help us to clean our environment by microbial bioremediation and to gradually increase agricultural profitability using microbial biocontrol agents and biofertilizers. Similarly, various potential microbes have critical roles in regulating the environment via their involvement production and consumption of greenhouse gases and other air pollutants from the environment. Microbes are potential and key natural agents for the removal and/or recycling of environmental contaminants.

Environmental pollutants such as industrial and pharmaceutical waste have emerged as global threats, creating widespread antibiotic resistance and giving rise to drug-resistant strains of pathogens. This book details the environmental problems posed by antibiotics, including the various types of toxic environmental pollutants discharged from both natural and anthropogenic activities and their toxicological effects on the environment, humans, animals, and plants. This book also highlights the recent advanced and innovative methods for the useful degradation and bioremediation of organic pollutants, heavy metals, dyes, etc. in the wastewater. In addition, this book covers a wide range of topics including environmental microbiology, biotechnology, nanotechnology, green chemistry, environmental science, and environmental engineering.

This book will also provide students, environmental scientists, environmental biotechnologists, microbiologists, biomedical scientists, and policymakers working in environmental microbiology, biotechnology, environmental sciences, and medical microbiology with the basic and advanced facts about the environmental issues and their challenges. Moreover, readers can also get state-of-art/background information on the existing environmental problems, their effects on human health, and suggested ways to control or contain their effects by employing various effective approaches.

The editors would like to express their sincere thanks to the contributors for submitting their work in a timely and proper manner. The editors are also thankful to national and international reviewers for evaluation and valuable suggestions and comments to raise the book’s quality for readers. Dr. Chowdhary acknowledges the support received from their family especially Father (Mr. Ram Chandra) and Mother (Mrs. Malti Devi). Furthermore, the editors also acknowledge the cooperation received from the Elsevier team and their guidance for finalizing this book.

Pankaj Chowdhary, Department of Microbiology, Babasaheb Bhimrao Ambedkar University, Lucknow, India

Abhay Raj, Environmental Microbiology Laboratory, Environmental Toxicology Group, CSIR-Indian Institute of Toxicology Research (CSIR-IITR), Lucknow, India

Digvijay Verma, Department of Microbiology, Babasaheb Bhimrao Ambedkar University, Lucknow, India

Yusuf Akhter, Department of Biotechnology, Babasaheb Bhimrao Ambedkar University, Lucknow, India

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 potential bioremediation. This chapter provides state-of-art information, as well as sources, productions, modes of action, and various industrial applications of LiP.

1.2 Production or sources of lignin peroxidase

Fungi and bacteria secrete one or more extracellular enzymes, that is, laccase, MnP, or LiP, that are essential for degradation of pollutants including lignin. LiP has been produced from various microbial sources, like fungi and bacteria. Lignin peroxidase activities have been shown by Streptomyces viridosporus, Thermobifida fusca, and actinomycetes (Bugg et al., 2011; Adav et al., 2010). Bacillus megaterium produced lignin peroxidase that has been isolated and identified based on morphological and biochemical tests. Further, physical parameters (pH, temperature, inoculum size, agitation speed) and nutritional parameters (carbon, nitrogen) were optimized. Finally, lignin peroxidase was filtered by ultrafiltration and purified by the ammonium sulfate and dialysis methods. The enzyme purification was checked by SDS-PAGE and its molecular weight was 6 kDa. Decolorization of the dyes like congo red (94.90%), methylene blue (63.23%), and malachite green (6.40%) was achieved by B. megaterium with an incubation period of 96 hours (Patil, 2014). Besides bacteria, some white-rot and brown-rot fungi have been also reported to possess ligninolytic capability. However, bacteria which can produce ligninases are classified as actinomycetes, α-proteobacteria, γ-proteobacteria (Bugg et al., 2011; Paliwal et al., 2012). Pant and Adholeya (2009) reported that maximum LiP production was found in Alternaria gaisen at about 137.42 U/g. LiP was also obtained from the Bacillus sp. cell extract, which was used for purification, fractionation, and characterization (Kharayat and Thakur, 2012). LiP occurs in some bacteria like Pseudomonas aeruginosa, Serretia marcescens, Nocardia, Arthrobacter, Flavobacterium, Phlebiaochraceofulva, Polyporous vercicolor and Agaricus bisporus and some frequently studied in white-rot fungus such as Phanerochaete chrysosporium, Dichomitus squaleus, Pleurotus ostreatus, Rigidoporus lignosus have proved to be an ideal microorganisms for the process of decolorization (Patil, 2014). Alternaria alternate (ANF238) was isolated from a sample of rotten wood for the production of LiP, using a lignocellulosic substrate (water hyacinth) under solid-state fermentation (Sharma et al., 2016).

Marine-derived fungi (Aspergillus sclerotiorum CBMAI 849, Cladosporium cladosporioides CBMAI 857 and Mucor racemosus CBMAI 847) under extraordinary carbon assets and salinity conditions releases enzymes MnP, LiP and laccase when cultured in malt extract supplement, however, production of these enzymes were not detected in basal medium supplemented with glucose and wheat bran. The outcomes showed high values of MnP and laccase beneath 12.5% and 23% (w/v) salinity, highlighting the capability of these fungi for industrial use and in the bioremediation of polluted areas with excessive salt concentrations. The very best values for LiP (75376.34 UI/L), MnP (4484.30 IU/L), and laccase (898.15 UI/L) were obtained with the fungus M. racemosus CBMAI 847 and it is by far the best option for ligninolytic enzymes production by using a zygomycete in this genus (Bonugli-Santos et al., 2009). In a further study, Carneiro et al. (2017) found that T. villosa has great potential in lignin degradation and other industrial applications.

1.3 Physiochemical and molecular properties lignin peroxidase

Ligninolytic enzymes, including LiP, have various physicochemical properties (Table 1–1). LiP is a monomeric hemoprotein (Khindaria et al., 1996). The isozyme of LiP ranges from 38 to 46 kDa with pI 3.2–4.0 and pH of about 3. The low optimum pH of LiP distinguishes it from other peroxidases. The ability of LiP is attributed to the acidic environment of Trp171 in P. chrysosporium LiP as it facilitates the stabilization of veratryl alcohol cation radicals (Khindaria et al., 1996). The crystal structure of P. chrysosporium LiP has been described (Poulos et al., 1993; Blodig et al., 2001). The enzyme is globular with a measurement of 50×40×40 Ǻ constructed from a proximal (C-terminal) and distal (N-terminal) area (Wong, 2009). The redox potential of LiPs (around 1.2 V at pH 3) makes these enzymes capable of oxidizing substrate that isn’t oxidized via other peroxidases (Sigoillot et al., 2012).

Table 1–1

Streptomyces viridosporus T7ALiP production and characterization has been studied There isn’t always a consensus regarding LiP molecular mass, as extraordinary data has been reported with the enzyme purification method. The molecular weight of the purified enzyme was 42 kDa as determined via SDS-PAGE. The Km values have been 54 and 76 μM for veratryl alcohol and H2O2, respectively. The pH and temperature optima have been 2.5°C and 25°C, respectively (Gottschalk et al., 2008). The pH and temperature optima of the LiP were 2.4°C and 22°C, respectively (Rai et al., 2016).

1.4 Mode of action

Lignin peroxidase has a standard catalytic cycle, which is similar to horseradish peroxidase in various aspects. According to Janusz et al. (2017) LiP catalytic mechanism is more similar to most of the available peroxidases. The most powerful class of LiP catalysis is a class II fungal peroxidase with the direct ability to oxidize dimeric lignin compounds like nonphenolic β-O-4 linkage-type arylglycerol-aryl ether (Scheme 1, reaction 2, substrate A) (Hofrichter et al., 2010).

During the LiP catalytic cycle, there are three steps, that is, one oxidation and two reduction steps:

In the first step there is 2e− oxidation of resting (native) ferric enzyme (LiP-Fe (III)) by hydrogen peroxide to form compound I oxo-ferryl intermediate (Fe-IV);

Further, during the second step an oxo-ferryl intermediate (lack of 2e−) is reduced by a molecule of substrate, such as nonphenolic aromatic substrate, which donates 1e− to compound I to form the second intermediate, compound II (lack of 1e−). Finally in the third step compound II returns to the resting ferric state, where the oxidation cycle ends with the gain of one or more electrons (e−) from the reducing substrate (Abdel-Hamid et al., 2013).

Compound I: The native lignin peroxidase reacts with H2O2 to form LiP-I with a second-order rate constant of 5.4×10⁵/M/S. The reaction can occur at pH 2.0–7.5 (Andrawis et al., 1988; Marquez et al., 1988).

The reason for the lack of any pH impact on the reaction isn’t clear. Hydrogen peroxide is the preferred substrate with a km value of ~30 µM, even though organic peroxides can function on the substrate, albeit with a decrease rate constant. The heterolytic cleavage of the Oα-Oβ bond of the peroxidase substrate is facilitated with the aid of the coordination of the heme Fe(III) and protonation by using the distal His47. The withdrawal of water leaves a brief Fe(III)-O+, observed using an electron system to form an oxyferryl complex Fe(IV)=O structure (Behere et al., 1985).

LiP-I therefore has a heme structure of O=Fe(IV)-porphyrin π radical cation with S=3/2. Over the native lignin peroxidase, it contains two oxidizing group; 1st located in the ferryl state of the Fe as [Fe(IV)=O] structure (low spin, S=1) and 2nd in the porphyrin π radical cation (S=1/2). Rather the heme radical, the participation of the surface Trp171 in a radical form via long-range electron transfer to the heme has also been suggested for H2O2-activated LiP (Blodig et al., 2001; Blodig et al., 1999).

Compound II

The reaction of LiP-I with a reducing substrate to form LiP-II is pH-dependent, with the charge reduced with increasing pH (Marquez et al., 1988; Tien et al., 1986). With veratryl alcohol as the substrate, the rate is 2.5×10⁶/M/S at pH 3.1 and reduces dramatically with increasing pH. The subsequent reaction of LiP-II with a second molecule of reducing substrate to yield the native enzyme is likewise pH structured and the rate is relatively slower (1.6×10⁵/M/S). The previous research findings clearly indicate that the pH dependence of the reduction of lignin peroxidase (LiP-I and LiP-II) rather than the development of LiP-I commandment the abnormal low pH optimum for the enzyme. In the first reduction step, the porphyrin π-cation radical first accepts an electron from the substrate, concomitant with a proton switch to the distal His. LiP-II thus formed is one oxidation equivalent above the native LiP, with the porphyrin filled by the donor substrate. The heme consequently has the shape of an oxyferryl complex hydrogen bonding with the protonated His, which then accepts an electron to form hydrogen bonds with the protonated His. This then accepts an electron from a second substrate, to yield the native LiP, as is known for different peroxidases (Ator and de Montelano, 1987).

Compound III

At pH 3.0 within the presence of extra H2O2 and the absence of a reducing substrate, LiP-II reacts with H2O2 to shape a catalytic inactive form of the enzyme, called compound III (LiP-III) (Marquez et al., 1988; Cai and Tien, 1992). The heme of LiP-III occurs as a ferric–superoxide complex Fe(III)O2−. LiP-III can be transformed to the resting enzyme by spontaneous autoxidation or using oxidation with a VA radical cation by the displacement of superoxide from the active site (Cai and Tien, 1992; Barr and Aust, 1994).

1.5 Application in various sectors

Ligninolytic enzymes gain more attention, in recent days due to their various biotechnological applications such as pulp and paper, cosmetics, bioethanol production, textiles, and biodegradation of many toxic phenolics and nonphenolic compounds present in the environment (Fig. 1–1 and Table 1–2).

Figure 1–1 Various applications of lignin peroxidase in industries and biotechnology.

Table 1–2

1.5.1 Cosmetic industry

In recent days various applications of lignin peroxidase have seen dramatical increases in use in many sectors. Woo et al. (2004) studied LiP purified from P. chrysosporium that was used in the decolorization of melanin (synthetic), and also its use in the production of new beauty lightening products. It demonstrated skin-lightening outcomes comparable to that of hydroquinone, without an observable adverse result, and with superiority in pores and skin texture and roughness (Draelos, 2015). The capability of LiP enzymes to oxidize a huge range of structurally distinctive substrates makes them a suitable agent for the oxidation of melanin that is structurally much like lignin. This enzyme with melanocytic capability has the potential for utility within the cosmetic manufacturing industries (Falade et al., 2017). Depigmentation and pores and skin-lightening products, which have been in use for a long time in Asian nations in which skin whiteness is the most important esthetic criterion, are also distinctly valued by the Western population, who suffer solar skin damage with expanded pores and skin spots (Couteau and Coiffard, 2016).

1.5.2 Bioethanol production

In recent year, ligninolytic fungi and enzymes (i.e., Lac, MnP, LiP) have been applied to the manufacturing of second-generation biofuels. Bioethanol is one of the most crucial biofuels manufactured from lignocellulosic matter. Generally, there are three steps involved in production from lignocellulosic materials, that is, (1) pretreatment, (2) saccharification, and (3) fermentation (Plácido and Capareda, 2015). The largest bioethanol producers in the world are the United States, Brazil, and China. In 2009 the United States produced 39.5×10⁹ L of ethanol using corn as a feedstock. At the same time the second one biggest producer, Brazil, created approximately 30×10⁹ L of ethanol using sugarcane. In recent years, China has been investing more in ethanol manufacturing and is one of its largest producers (Ivanova et al., 2011). In India, the investigations into biofuels are developing in order to replace oil to achieve power protection and to promote an agricultural boom. Indian authorities are aiming to achieve a target of 20% mixing of fossil fuels with biodiesel and bioethanol (Saini et al., 2014). Further, a countrywide policy for biofuel has been framed which includes promoting biofuel manufacturing, in particular on wastelands (Ravindranath et al., 2011). In biofuel manufacturing, the ligninolytic enzymes have two primary purposes, delignification, and cleansing. Delignification techniques apply ligninolytic fungus and their enzymes to reduce the lignin content material in several feedstocks (Salvachúa et al., 2011; Nigam et al., 2009; Lu et al., 2010). Detoxification process utilizes the ligninolytic enzymes (LiP, MnP, laccase) to mitigate or remove the toxic pollutants present in the biomass hydrolysates after chemical or physico-chemical parameters (Jönsson et al., 1998; Chandel et al., 2007). Well-studied fungi like P. chrysosporium, Pycnoporus cinnarbarinus, Pleurotus ostreatus, Trametes pubescens, Ceriporiopsis subvermispora, and Cyathus stercolerus have shown more delignification potential (Kumar et al., 2009; Sahu and Pramanik, 2015).

1.5.3 Pulp and paper industry

The pulp industry usually generates a huge volume of effluent, which represents significant environmental and economic concerns. The wastewater discharge from small-scale paper industries has high (2.5 times) biochemical oxygen demand, in comparison to large-scale paper industries. Per annum, these industries produce approximately 1 million tons of all types of papers. The pulping by-product (black liquor) and pulp mill wastewater pose extreme environmental problems because of their excessive pollutant loads. Fixing the pulp and paper industries’ environmental issues is critical to retaining the forest industries and helpful for converting the financial needs of the forest communities (Khalid et al., 2009). Organic methods for the remedy of black liquor using a biological agent, like fungi, bacteria, algae, and enzymes, in a single-step process or in combination with other physical and chemical methods seem to be more effective and eco-friendly (Chandra et al., 2011).

Amongst the biological strategies attempted so far, most of the literature is restricted to a few genera of white-rot fungi due to their nonspecific extracellular enzymatic system (LiP, MnP, Lac) that is used in LiP biodegradation (Hammel and Cullen, 2008). Paper mill sludges are notably varied in composition, even between producers using the identical pulp and paper manufacturing manner. PMS is polysaccharide material—cellulose, lignin, and hemicellulose (Jackson and Line, 2009). Pulp manufacturing in pulp paper industries involves two major strategies, that is, wood digestion and biobleaching. Within the technique of wood digestion, wood chips are cooked inside a solution of NaOH and NaSO4 at increased temperature and pressure to break down the chips into a fiber mass. The chemical reaction with wood fibers dissolves all of the depository substances which are hard to degrade and these derivatives are washed far away from the fiber at some stage in the washing and dewatering process. The various extracts in the course of washing consist of specifically lignins, cellulose, phenolics resins, fatty acids, and tannins blended to make a dark black viscous alkaline waste called black liquor. The discharge effluent contains about 10-15% alkaline part of total wastewater but contributes in almost above 90-95% of the pollution load in terms of high pH, BOD, COD and colour which severely affect the environment (Grover et al., 1999).

1.5.4 Textile industry

The textile industry uses a number of synthetic dyes during processing, and these dyes are the principal sources of environment pollutants (Singh et al., 2015). Parshetti et al. (2012) reported that purified LiP from Kocuria rosea MTCC 1532 decolorized 11 special dyes belonging to numerous structural groups; azo, triphenyl-methane, heterocyclic, polymeric, and metallic complexes. Synthetic dyes released by various textile industries are a source of concern to environment safety. Existing physicochemical methods of dye removal from effluents have disadvantages like excessive operational value, low efficiency, and production of a huge quantity of sludge (Shinkafi et al., 2015).

1.6 Miscellaneous biotechnological application

The various applications of LiP consist of delignification of feedstock for ethanol manufacturing, fabric effluent remediation, dye decolorization, coal depolymerization, treatment of hyperpigmentation, and skin-lightening through melanin oxidation. There is potential utility of LiP in skin-lightening functions via novel mechanisms, therefore it holds high value for the cosmetics sector where it can function as suitable alternative to hydroquinone; a powerful skin-lightening agent whose safety has generated major controversy (Falade et al., 2017). A large amount of lignocellulosic waste generated using forestry, agricultural practices, paper pulp industries, and fabric/dye-stuff industries poses an intense environmental pollutants problem. Paper manufacturing facility effluent is one of the foremost pollutants on Earth because it is highly colored. The persistent darkish brown coloration is because of dissolved lignin-based totally synthetic, aromatic, and chlorinated compounds derived from the condensate, pulp washing, chlorine and alkali bleach waste, black liquor spillage, and foul evaporator condensate (Jadhav et al., 2016). The ligninolytic enzyme system of microbes has been implicated in the degradation of numerous xenobiotics, which include chlorophenols, PAHs, organophosphorus, and phenols (Marco-Urrea and Reddy, 2012; Tisma et al., 2010).

1.7 Conclusion and future prospects

Today, development is rapidly increasing worldwide in many sectors. Undoubtedly, ligninolytic enzymes including lignin peroxidase have ample opportunities and applications in various sectors. An effective ligninolytic enzyme production system is necessary for biotechnological applications, and therefore, a deeper knowledge of physicochemical and molecular mechanisms is essential for the transcriptional regulation of every ligninolytic enzyme, including LiP. The capability of peroxidase (LiP) is severe and the issues are difficult to resolve. In spite of its low operational stability, peroxidase can be an efficient biocatalyst for the production of industrially applicable compounds.

Because of the tremendous significance and potential applications of LiP, further study of the underexplored microbial range for new LiPs with more advantageous skills is essential. The necessity of lignin peroxidase for bioremediation of toxic pollutants, use in cosmetics and new drugs discovery, employment, and financial system may be need more focused research.

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2

Microbes mediated approaches for environmental waste management

Sujata Mani¹, Pankaj Chowdhary² and Surabhi Zainith²,    ¹1Department of Biochemistry, Gramin Science (Vocational) College, Vishnupuri, Nanded, Maharashtra, India,    ²2Department of Microbiology, Babasaheb Bhimrao Ambedkar University (A Central University), Lucknow, India

Abstract

Microorganisms serve as an affirmative role in making humans’ life much better and easier by maintaining numerous natural as well as man-made singularities in the environment. One of the most important areas where microbes give their best results is in the management of waste. Nowadays, the most challenging undertaking that environmental agencies and government face is the proper discarding of the waste generated from different human activities. The most successful way of contending with this waste disposable hazard is through the use of microbes including bacteria, fungi, algae, etc. Thus this chapter deals with the various eco-friendly processes through which the hazardous wastes that are generated from different sources, such as municipal waste, industrial waste, medical waste, radioactive waste, etc., which are harmful for the environment and humans, can be managed efficiently. This chapter also deals with the characteristics and classifications of the waste generated in the ecosystem and the various types of management techniques. This chapter also shows the most specific and efficient ways of using microorganisms through bioremediation, bioaugumentation, etc., for the management of waste.

Keywords

Hazardous waste; municipal; industrial; radioactive; management; microorganisms; bioremediation; bioaugumentation

2.1 Introduction

The unwanted by-products or residues obtained as a result of any negative value discarded from the place of its production is referred to as waste material. These are the materials or substances which are meant to be discarded or have been already discarded due to their hazardous properties, when generated from any kind of industry. The substances or materials regarded as wastes may be in solid, liquid, and gaseous form, and are generally released as domestic waste, sewage sludge, manufacturing industries activities, electronic scraps, nuclear waste, industrial wastewaters, etc. (Angulo et al., 2010; Hassan et al., 2003). These wastes in different forms tend to change in different toxic or hazardous forms over a period of time after disposal. Solid wastes include common domestic wastes (such as kitchen and garden area), industrial waste, sewage sludge, construction and destruction area wastes, agricultural area wastes, mining wastes, food processing wastes, petroleum wastes, etc. (Demirbas, 2011). Liquid wastes include domestic wastewater, for example, bathroom, laundry, and liquid kitchen waste, used oils, stormwater, and wastewater generated during industrial processes, whereas gaseous wastes comprise small particles and gases emitted from vehicles, open fires, incinerators, or produced by agricultural and industrial processes. Once these gases and particles are released into the environment, they become too hard to control and