China 
Africa 
Explore chapters and articles related to this topic
Lignocellulosic Biomass Wastes to Bioenergy
Published in Amit Kumar, Chhotu Ram, Nanobiotechnology for Green Environment, 2021
Amit Kumar, Diwakar Aggarwal, Amit Kumar Bharti, Chhotu Ram
Lignin degradation is performed by white-rot fungi most effectively. Lignin peroxidases, manganese peroxidizes, and laccases are the major lignin-degrading enzymes that are produced by these fungi. The characteristics of these enzymes vary according to the microbial source. Lignin peroxidase is also known as ligninase. It is one of the most important enzymes involved in the degradation of lignin. Lignin peroxidase has high redox potential (700–1,400 mV) and it can degrade the compounds with high redox potential that are not oxidized by other enzymes. Lignin peroxide can oxidize both phenolic and non-phenolic compounds. It can cleave the recalcitrant non-phenolic units that comprise approximately 90% of lignin (Niladevi, 2009; Plácido and Capareda, 2015). Manganese peroxidase is another important enzyme produced by the lignin-degrading fungi. It is also a heme peroxidase and requires H2O2 for its activity. Manganese peroxidase has lower redox potential lignin peroxidase and generally, it does not oxidize non-phenolic lignin compounds. They are glycoproteins with a molecular weight between 38 and 62.5 kDa (Niladevi, 2009; Plácido and Capareda, 2015). Laccases are the multicopper oxidase enzyme, widely distributed in plants, fungi, and bacteria and have the ability to catalyze the oxidation of various phenolic and non-phenolic compounds as well as many environmental pollutants (Dwivedi et al., 2011).
*
Published in Eli Ruckenstein, Hangquan Li, Chong Cheng, Concentrated Emulsion Polymerization, 2019
Eli Ruckenstein, Xiao-Bai Wang
The ligninase was first identified as an extracellular oxygenase7,8 and later as multiple peroxidases.9–12 The production of lignin peroxidases in agitated shake cultures is enhanced by veratryl alcohol.13 This observation was followed by a report that immobilized Phanerochaete chrysosporium can be efficient in producing extracellular lignin peroxidase.14 Numerous carriers have been tried for the immobilization of Phanerochaete chrysosporium, such as nylon web,15–27 polyurethane foam,17,22,28–34 silicon tubing,35,36 sintered glass,37 porous ceramics,38 polypropylene,39 stainless steel,10,39 agarose,14,22 and agar gel beads.14,22 Good results have been obtained with nylon web, polyurethane foam, sintered glass, or silicon tubing as carriers. In the present study, a new carrier, namely porous poly(styrene-divinylbenzene) prepared by the concentrated emulsion polymerization method,40,41 is investigated.
Role of Microbes in Solid Waste Management
Published in Ashok K. Rathoure, Zero Waste, 2019
Peroxidases are involved in diverse biological reactions and are often categorized as haem and non-haem proteins. These catalyse the oxidation of phenolics and lignins at the expense of hydrogen peroxide. Based on their source and activity, peroxidases have been classified into lignin peroxidase, manganese-dependent peroxidase and versatile peroxidase. Lignin peroxidase participate in the degradation of lignin, a constituent of plant cell wall. It also oxidizes aromatic compounds and plays a key role in aromatic waste management. However, the mechanism of action is still not well understood (Piontek et al., 2001).
Impact of nanomaterials accumulation on the organic carbon associated enzymatic activities in soil
Published in Soil and Sediment Contamination: An International Journal, 2023
Gyan Datta Tripathi, Zoya Javed, Meghana Gattupalli, Kavya Dashora
Enzymes play a very important role in lignin degradation and divided into two main groups: Lignin modifying enzyme (LME), phenol oxidase (laccases) and heme containing peroxidases (POD), particularly lignin, manganese, and multifunctional (versatile) peroxidase, are two types of LME generated by bacteria and the next is lignin degrading auxiliary (LDA) are unable to breakdown lignin on their own (da Silva Coelho-Moreira et al. 2013). Lignin peroxidase (LiP, EC 1.11.1.14) is a glycosylated enzyme that uses hydrogen peroxide (H2O2) to catalyze the oxidation of non-phenolic lignin units and mineralize resistant aromatic chemicals. Lignin oxidation occurs through electron transfer, non-catalytic bond cleavages, and aromatic ring opening (Choinowski, T et al. 1999). . During the early phases of lignin breakdown, the enzyme Manganese peroxidase (MnP,EC 1.11.1.13) plays a critical role (Perez, J et al. 1990).Due to its larger redox potential, MnP promotes more phenolic lignin breakdown than laccase, resulting in the release of carbon dioxide (Ten Have, R., & Teunissen, P. J. 2001). Versatile Peroxidase (VP, EC 1.11.1.16) as the name implies, versatile peroxidase has both LiP and MnP catalytic capabilities. VP was originally extracted from the Bjerkandera fungi, and it was discovered that it could alter lignin without the use of an external mediator (Moreira, P. R et al.2007).
Endocrine disrupting chemicals (EDCs): chemical fate, distribution, analytical methods and promising remediation strategies – a critical review
Published in Environmental Technology Reviews, 2023
Mridula Chaturvedi, Sam Joy, Rinkoo Devi Gupta, Sangeeta Pandey, Shashi Sharma
Lignin peroxidase (LiP) is heme-containing an extracellular enzyme, also known as ligninase, secreted by white rot fungi during secondary metabolism. LiPs have isoelectric point (pI) between 3.1 and 4.7 and optimum activities between pH (2–5) and temperature (35–55°C). The natural mediator that improves enzyme activities is veratyl alcohol. LiP does not need mediators as laccases to eliminate high redox-potential compounds but it involves hydrogen peroxide to initiate the catalysis. LiP activity is inhibited by hydroxyl amino-dinitrotoluene, EDTA, sodium azide and mercaptoethanol [147].