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Cited by 648Enzyme-mediated dye degradationLignin and Wood ChemistryEnzyme Production and Characterization

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Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment

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Kumar, Adarsh, Chandra, Ram·2020·Heliyon
DOI 10.1016/j.heliyon.2020.e03170PMC PMC7033530
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Abstract

Ligninolytic enzymes play a key role in degradation and detoxification of lignocellulosic waste in environment. The major ligninolytic enzymes are laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase. The activities of these enzymes are enhanced by various mediators as well as some other enzymes (feruloyl esterase, aryl-alcohol oxidase, quinone reductases, lipases, catechol 2, 3-dioxygenase) to facilitate the process for degradation and detoxification of lignocellulosic waste in environment. The structurally laccase is isoenzymes with monomeric or dimeric and glycosylation levels (10–45%). This contains four copper ions of three different types. The enzyme catalyzes the overall reaction: 4 benzenediol + O 2 to 4 benzosemiquinone + 2H 2 O. While, lignin peroxidase is a glycoprotein molecular mass of 38–46 kDa containing one mole of iron protoporphyrin IX per one mol of protein, catalyzes the H 2 O 2 dependent oxidative depolymerization of lignin. The manganese peroxidase is a glycosylated heme protein with molecular mass of 40–50kDa. It depolymerizes the lignin molecule in the presence of manganese ion. The versatile peroxidase has broad range substrate sharing typical features of the manganese and lignin peroxidase families. Although ligninolytic enzymes have broad range of industrial application specially the degradation and detoxification of lignocellulosic waste discharged from various industrial activities, its large scale application is still limited due to lack of limited production. Further, the extremophilic properties of ligninolytic enzymes indicated their broad prospects in varied environmental conditions. Therefore it needs more extensive research for understanding its structure and mechanisms for broad range commercial applications.

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Metadata

Authors
Kumar, A., & Chandra, R.
Affiliations
Babasaheb Bhimrao Ambedkar University (IN)
Corresponding author
Chandra, Ram
ORCID
Kumar, Adarsh
Venue
Heliyon
Publisher
Elsevier BV
Published
2020-02
Volume
6
Issue
2
Pages
e03170
ISSN
2405-8440 (ISSN-L)
DOI
10.1016/j.heliyon.2020.e03170
PMC
PMC7033530
OpenAlex
W3006791941
Cited by
648
References
2
Citations by year
2026: 103 · 2025: 137 · 2024: 124 · 2023: 116 · 2022: 72 · 2021: 79 · 2020: 17
FWCI
6.07
Type
journal article
Language
en
Open access
Licence
Locations
  • Heliyon (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • University Grants Commission
  • Department of Biotechnology, Ministry of Science and Technology, India (BT/PR18896/BCE/8/1372/2016)
Topics
  • Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Enzyme-mediated dye degradation
  • Physical Sciences › Chemical Engineering › Process Chemistry and Technology › Lignin and Wood Chemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords
ligninolytic enzymes, lignin degradation, lignocellulosic waste, manganese peroxidase, versatile peroxidase, oxidative depolymerization, heme proteins, extremophilic enzymes, enzyme production

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