In the presented work 6 different oxidoreductases were investigated for their potential to specifically decolorize 207 industrially relevant dyes including anthraquinone-, azo-, trimethylmethane-, and indigo chromophores. Utilized enzymes were cellobiose dehydrogenase from the plant-pathogenic fungus Sclerotium rolfsii, laccases from the ascomycete Botrytis aclada and the basidiomycete Trametes pubescens, glucose oxidase from Aspergillus niger, glucose dehydrogenase from Glomerella cingulata and horseradish peroxidase. Decolorization was studied at alkaline, neutral or acidic pH using UV/vis spectroscopy in the 96-well plate format. Absorbances of most of the investigated dyes could be reduced by at least 50% within 48 hours of incubation at room temperature. Highest rates of decolorization were observed at pH 4 for most of the enzymes. Horseradish peroxidase efficiently degraded 79 out of 175 dyes diluted in water (45%) followed by laccase from T. pubescens (27%), laccase from B. aclada (27%), cellobiose dehydrogenase (15%) and glucose dehydrogenase (5.7%). Glucose oxidase (4%) was least successful, indicating that peroxide has little effect on the chromophores. Highest specific enzyme activities of 1590 and 1718 U/mg were achieved with Acid Blue 45 when reacted with laccase from T. pubescens and HRP. Our results show that with a limited number of enzymes a multitude of dyes can be effectively decolorized. Toxic effects of the dyes on freshwater algae were also studied to assess their environmental impact.