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Characterization of Plant Peroxidases and Their Potential for Degradation of Dyes: a Review

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Abstract

Peroxidases are ubiquitously found in all vascular plants and are promising biocatalysts for oxidization of wide range of aromatic substrates including various industrial dyes. Peroxidases can catalyze degradation of chemical structure of aromatic dyes either by precipitation or by opening the aromatic ring structure. Both soluble and immobilized peroxidases have been successfully used in batches as well as in continuous processes for the treatment of aromatic dyes present in industrial effluents. Plant peroxidases are stable catalysts that retain their activities over a broad range of pH and temperatures. The performance of an enzyme for degradation process depends upon the structure of dyes and the operational parameters like concentration of enzyme, H2O2 and dye, incubation time, pH, and temperature. Recalcitrant dyes can also be mineralized by plant peroxidases in the presence of redox mediators. Thus, plant peroxidases are easily available, inexpensive, and ecofriendly biocatalysts for the treatment of wastewaters containing a wide spectrum of textile and non-textile synthetic dyes. This article reviews the recent developments in isolation and characterization of plant peroxidases and their applications for bioremediation of synthetic dyes.

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Authors and Affiliations

  1. Department of Chemistry, Govt College Women University, Faisalabad, Pakistan

    Umme Kalsoom

  2. Environmental & Material Chemistry Laboratory, Department of Chemistry, University of Agriculture, Faisalabad, 38040, Pakistan

    Haq Nawaz Bhatti

  3. Department of Biochemistry, University of Agriculture, Faisalabad, 38040, Pakistan

    Muhammad Asgher

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  1. Umme Kalsoom
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  2. Haq Nawaz Bhatti
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  3. Muhammad Asgher
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Correspondence to Haq Nawaz Bhatti.

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Kalsoom, U., Bhatti, H.N. & Asgher, M. Characterization of Plant Peroxidases and Their Potential for Degradation of Dyes: a Review. Appl Biochem Biotechnol 176, 1529–1550 (2015). https://doi.org/10.1007/s12010-015-1674-3

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  • DOI: https://doi.org/10.1007/s12010-015-1674-3

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