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Peroxidase enzymes as green catalysts for bioremediation and biotechnological applications: A review

Sellami, Kheireddine, Couvert, Annabelle, Nasrallah, Noureddine, Maachi, Rachida, Abouseoud, Mahmoud, Amrane, Abdeltif·2022·Science of The Total Environment
DOI 10.1016/j.scitotenv.2021.150500
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Abstract

The fast-growing consumer demand drives industrial process intensification, which subsequently creates a significant amount of waste. These products are discharged into the environment and can affect the quality of air, degrade water streams, and alter soil characteristics. Waste materials may contain polluting agents that are especially harmful to human health and the ecosystem, such as the synthetic dyes, phenolic agents, polycyclic aromatic hydrocarbons, volatile organic compounds, polychlorinated biphenyls, pesticides and drug substances. Peroxidases are a class oxidoreductases capable of performing a wide variety of oxidation reactions, ranging from reactions driven by radical mechanisms, to oxygen insertion into CH bonds, and two-electron substrate oxidation. This versatility in the mode of action presents peroxidases as an interesting alternative in cleaning the environment. Herein, an effort has been made to describe mechanisms governing biochemical process of peroxidase enzymes while referring to H 2 O 2 /substrate stoichiometry and metabolite products. Plant peroxidases including horseradish peroxidase (HRP), soybean peroxidase (SBP), turnip and bitter gourd peroxidases have revealed notable biocatalytic potentialities in the degradation of toxic products. On the other hand, an introduction on the role played by ligninolytic enzymes such as manganese peroxidase (MnP) and lignin peroxidase (LiP) in the valorization of lignocellulosic materials is addressed. Moreover,…

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Metadata

Authors
Sellami, K., Couvert, A., Nasrallah, N., Maachi, R., Abouseoud, M., & Amrane, A.
ORCID
Sellami, Kheireddine
Venue
Science of The Total Environment
Publisher
Elsevier BV
Published
2022-02
Volume
806
Pages
150500
ISSN
0048-9697
DOI
10.1016/j.scitotenv.2021.150500
Cited by
205
References
2
Language
en
Licence
Funders
  • République Algérienne Démocratique et Populaire Ministère de l'enseignement supérieur et de la recherche scientifique (933290A)
  • Campus France

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