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Additional file 1: of A novel starch-binding laccase from the wheat pathogen Zymoseptoria tritici highlights the functional diversity of ascomycete laccases

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posted on 2019-08-20, 04:13 authored by Majid Haddad Momeni, Paolo Bollella, Roberto Ortiz, Esben Thormann, Lo Gorton, Maher Abou Hachem
Table S1. Septoria cluster laccases. Figure S1. Chemical structure of the osmium polymer. Figure S2. Activity screening on aromatic (mainly phenolics) susbtrates. Figure S3. ZtrLac1A primary structure and purification. Figure S4. Cyclic voltammograms. Figure S5. Sequence alignment of ZtrLac1A and homologues from AA1_3. Figure S6. Architecture of Cu1 copper site in characterized ascomycetes laccases. (PDF 747 kb)

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Novo Nordisk Fonden (DK)

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    BMC Biotechnology

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    Carbohydrate binding module family 20 (CBM20)Cyclic voltammogramsLaccaseOxidoreductasePlantPathogenStarchZymoseptoria tritici

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