Improving the pH-stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase
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Improvement of catalytic performance of lignin peroxidase for the enhanced degradation of lignocellulose biomass based on the imbedded electron-relay in long-range electron transfer routeLimits of Versatility of Versatile Peroxidase.Correction: Improving the pH-stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase.Rational design of Pleurotus eryngii versatile ligninolytic peroxidase for enhanced pH and thermal stability through structure-based protein engineering.Enzyme activities of two recombinant heme-including peroxidases TvDyP1 and TvVP2 identified from the secretome of Trametes versicolor.
P2860
Improving the pH-stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase
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name
Improving the pH-stability of ...... ly-Stable Manganese Peroxidase
@ast
Improving the pH-stability of ...... ly-Stable Manganese Peroxidase
@en
type
label
Improving the pH-stability of ...... ly-Stable Manganese Peroxidase
@ast
Improving the pH-stability of ...... ly-Stable Manganese Peroxidase
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prefLabel
Improving the pH-stability of ...... ly-Stable Manganese Peroxidase
@ast
Improving the pH-stability of ...... ly-Stable Manganese Peroxidase
@en
P2093
P2860
P1433
P1476
Improving the pH-stability of ...... ly-Stable Manganese Peroxidase
@en
P2093
Antonio Romero
Elena Fernández-Fueyo
Francisco Javier Medrano
Verónica Sáez-Jiménez
P2860
P304
P356
10.1371/JOURNAL.PONE.0140984
P407
P577
2015-10-23T00:00:00Z