Abstract
Five fractions with lignin peroxidase activity were isolated by FPLC-Mono Q from a Streptomyces viridosporus culture. F4 and F5 showed the highest specific activity and degree of protein homogeneity by chromatofocusing, IEF- and gradient-PAGE. The individual analysis of F4 and F5 by FPLC-Superdex 75, showed MW that were multiples to each other (68,000; 23,000; 12,000), although by SDS PAGE a sole MW of 13,500 was obtained, indicating a monomer based structure. The amino-acid composition of F5 showed absence of sulfur amino acids.
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Bon, E.P., Nascimento, H.J., Macedo, J.M. et al. Lignin peroxidase isoforms from Streptomyces viridosporus T7A: are they a monomer based structure?. Biotechnology Techniques 13, 289–293 (1999). https://doi.org/10.1023/A:1006914312208
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DOI: https://doi.org/10.1023/A:1006914312208