Laccase kinetics of degradation and coupling reactions

Zille, Andrea; Munteanu, Florentina-Daniela; Gübitz, Georg; Cavaco‐Paulo, Artur

doi:10.1016/j.molcatb.2005.01.005

Cited by 42 publications

(24 citation statements)

References 49 publications

(45 reference statements)

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“…The rate of decolorization for methyl orange and Bismarck brown was 71% and 75%, respectively. The improved degradation of the azo dye, methyl orange, by the laccase-HOBT system has been reported (28). In the present study, it was observed that the laccase-HOBT system could decolorize acid orange and Bismarck brown more efficiently than methyl orange.…”

Section: Dye Decolorization Studiessupporting

confidence: 62%

Strategies for Enhancing Laccase Yield from Streptomyces psammoticus and Its Role in Mediator-based Decolorization of Azo Dyes

Niladevi

Sheejadevi

Prema

2008

Appl Biochem Biotechnol

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Enhanced production of laccases from Streptomyces psammoticus in solid-state fermentation was carried out using two different strategies: laccase inducers and scale-up process. Laccase yield was enhanced by a wide range of aromatic inducers. The best inducer was pyrogallol, which yielded 116 U/g as compared to the control (55.4 U/g). Scale-up studies in packed bed bioreactor was performed at different aeration rates. Aeration at 1.5 vvm was identified as the optimum condition for laccase production (75.4 U/g) in the column bioreactor. The enzyme yield was enhanced further by combining the best conditions from the first two experiments. Fermentation was carried out in bioreactors in the presence of 1 mM pyrogallol, which resulted in 3.9-fold increase in laccase yield (215.6 U/g). The role of laccase in azo dye decolorization was evaluated in the presence of four different laccase mediators, at different concentrations. 1-Hydroxybenzotriazole (HOBT) proved to be the best mediator for S. psammoticus laccase and decolorized the azo dyes efficiently. Acid orange, Methyl orange, and Bismarck brown were decolorized at the rates of 86%, 71%, and 75% respectively, by HOBT.

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Section: Dye Decolorization Studiessupporting

confidence: 62%

Strategies for Enhancing Laccase Yield from Streptomyces psammoticus and Its Role in Mediator-based Decolorization of Azo Dyes

Niladevi

Sheejadevi

Prema

2008

Appl Biochem Biotechnol

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“…The remediation of textile effluents remains a challenge in wastewater treatment. Biotechnologies based on the catalytic reactions of laccases represent efficient approaches for the treatment of dyeing wastewaters (Abadulla et al 2000;Blánquez et al 2004;Husain 2006;Benzina et al 2013;Khouni et al 2010;Pereira et al 2009;Chivukula and Renganathan 1995;Zille et al 2005;Murugesan et al 2009). The laccase-induced dye transformation processes are considered environmental friendly since the oxidation occurs through a highly non-specific free radical mechanism, forming phenolic type compounds and prohibiting the formation of toxic aromatic amines (Pereira et al 2009;Chivukula and Renganathan 1995;Zille et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Potential of acetylacetone as a mediator for Trametes versicolor laccase in enzymatic transformation of organic pollutants

Yang

Sun

Zhang

et al. 2015

Environ Sci Pollut Res

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Low-cost and environmentally friendly mediators could facilitate the application of laccase (EC 1.10.3.2) in variant biotechnological processes. Acetylacetone (AA) represents an inexpensive and low toxic small molecular diketone that has been proven as an effective mediator for laccase in free radical polymerization. However, the potential of AA as a mediator for laccase in pollutant detoxification and/or degradation is still unknown. In this work, the roles of AA in laccase-induced polymerization and transformation were investigated. AA was demonstrated to be a highly efficient mediator in the laccase-induced grafting copolymerization of acrylamide and chitosan. The efficacy of AA in the laccase-induced decoloration of malachite green (MG) was compared with that of the widely used 1-hydroxybenzotriazole (HBT). The laccase-AA system had the highest turnover number (TON, 39.1 μmol/U), followed by the laccase-only system (28.5 μmol/U), while the TON of the laccase-HBT system was the lowest (14.9 μmol/U). The pseudo-first-order transformation rate constant (k 1) of MG in the laccase-AA system was up to 0.283 h(-1) under the given conditions, while the k 1 of AA caused by laccase was only 0.008 h(-1). In the five-cycle run, the concentration of AA remained stable. The larger TON of the laccase-AA system and the stability of AA in the cycling runs demonstrate that AA was more recyclable than HBT in the LMS, leading to a prolonged serving life of laccase. These results suggest that AA might be a potential redox mediator for laccase.

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“…The enzymes are able to break specific chemical bonds in a wide variety of commercial dye molecules. According to current knowledge, enzymes laccase, manganese peroxidase and lignin peroxidase play a major role in decolourization [4,5]. Manganese peroxidase and lignin peroxidase have been studied in a connection with the degradation of polyaromatic dyes [6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%