Literature DB >> 12675567

Oxidative degradation of azo dyes by manganese peroxidase under optimized conditions.

I Mielgo1, C López, M T Moreira, G Feijoo, J M Lema.   

Abstract

The application of enzyme-based systems in waste treatment is unusual, given that many drawbacks are derived from their use, including low efficiency, high costs and easy deactivation of the enzyme. The goal of this study is the development of a degradation system based on the use of the ligninolytic enzyme manganese peroxidase (MnP) for the degradation of azo dyes. The experimental work also includes the optimization of the process, with the objective of determining the influence of specific physicochemical factors, such as organic acids, H(2)O(2) addition, Mn(2+) concentration, pH, temperature, enzyme activity and dye concentration. A nearly total decolorization was possible at very low reaction times (10 min) and at high dye concentration (up to 1500 mg L(-)(1)). A specific oxidation capacity as high as 10 mg dye degraded per unit of MnP consumed was attained for a decolorization higher than 90%. Among all, the main factor affecting process efficiency was the strategy of H(2)O(2) addition. The continuous addition at a controlled flow permitted the progressive participation of H(2)O(2) in the catalytic cycle through a suitable regeneration of the oxidized form of the enzyme, which enhanced both the extent and the rate of decolorization. It was also found that, in this particular case, the presence of a chelating organic acid (e.g., malonic) was not required for an effective operation. Probably, Mn(3+) was chelated by the dye itself. The simplicity and high efficiency of the process open an interesting possibility of using of MnP for solving other environmental problems.

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Year:  2003        PMID: 12675567     DOI: 10.1021/bp020136w

Source DB:  PubMed          Journal:  Biotechnol Prog        ISSN: 1520-6033


  8 in total

Review 1.  Recent advances in azo dye degrading enzyme research.

Authors:  Huizhong Chen
Journal:  Curr Protein Pept Sci       Date:  2006-04       Impact factor: 3.272

2.  The role of Mn-dependent peroxidase in dye decolorization by static and agitated cultures of Irpex lacteus.

Authors:  K Svobodová; P Erbanová; J Sklenár; C Novotný
Journal:  Folia Microbiol (Praha)       Date:  2006       Impact factor: 2.099

3.  Peroxidase-producing actinobacteria from Algerian environments and insights from the genome sequence of peroxidase-producing Streptomyces sp. S19.

Authors:  Rima Maibeche; Nawel Boucherba; Kamel Bendjeddou; Alaric Prins; Cilia Bouiche; Samir Hamma; Mohammed Benhoula; Zahra Azzouz; Azzeddine Bettache; Said Benallaoua; Marilize Le Roes-Hill
Journal:  Int Microbiol       Date:  2022-01-20       Impact factor: 2.479

4.  Pleurotus ostreatus manganese-dependent peroxidase silencing impairs decolourization of Orange II.

Authors:  Tomer M Salame; Oded Yarden; Yitzhak Hadar
Journal:  Microb Biotechnol       Date:  2009-11-11       Impact factor: 5.813

5.  Expression and characteristics of manganese peroxidase from Ganoderma lucidum in Pichia pastoris and its application in the degradation of four dyes and phenol.

Authors:  Hui Xu; Meng-Yuan Guo; Yan-Hua Gao; Xiao-Hui Bai; Xuan-Wei Zhou
Journal:  BMC Biotechnol       Date:  2017-02-23       Impact factor: 2.563

6.  Heterologous Expression of Phanerochaete chrysoporium Glyoxal Oxidase and its Application for the Coupled Reaction with Manganese Peroxidase to Decolorize Malachite Green.

Authors:  Yu-Lim Son; Hyoun-Young Kim; Saravanakumar Thiyagarajan; Jing Jing Xu; Seung-Moon Park
Journal:  Mycobiology       Date:  2012-12-26       Impact factor: 1.858

Review 7.  Linking Enzymatic Oxidative Degradation of Lignin to Organics Detoxification.

Authors:  Xiaolu Wang; Bin Yao; Xiaoyun Su
Journal:  Int J Mol Sci       Date:  2018-10-28       Impact factor: 5.923

8.  Fe-Loaded MOF-545(Fe): Peroxidase-Like Activity for Dye Degradation Dyes and High Adsorption for the Removal of Dyes from Wastewater.

Authors:  Chuang Zhang; Haichao Li; Chen Li; Zhengqiang Li
Journal:  Molecules       Date:  2019-12-31       Impact factor: 4.411

  8 in total

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