• Characterization of bacterial dye-decolorizing peroxidases = Bakteriaalsete värvi pleegitavate peroksüdaaside iseloomustaminePupart, Hegne2024 https://www.ester.ee/record=b5713840*est https://digikogu.taltech.ee/et/Item/d40055e9-2600-4e49-8aec-3f561267772e https://doi.org/10.23658/taltech.72/2024
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• Dye-decolorizing peroxidases from Streptomyces coelicolor show organosolv lignin remodeling activityPupart, Hegne; Ojangu, Eve-Ly; Zovo, Kairit; Lukk, TiitFEBS Open Bio2021 / p. 63 https://febs.onlinelibrary.wiley.com/doi/epdf/10.1002/2211-5463.13206 https://doi.org/10.1002/2211-5463.13206
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