A highly stable laccase obtained by swapping the second cupredoxin domain

• Published in: Scientific reports Vol. 8; no. 1; pp. 15669 - 10
• Main Authors: Pardo, Isabel, Rodríguez-Escribano, David, Aza, Pablo, de Salas, Felipe, Martínez, Angel T., Camarero, Susana
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 23.10.2018; Nature Publishing Group; Nature Portfolio
• Subjects: 38/22; 38/23; 38/77; 42/44; 42/70; 631/45/603; 631/45/607/1168; 631/61/338/469; 82/80; 82/81; 82/83; Amino acid sequence; Cupredoxin Domains; Enzymes; Ethanol; Glycosylation; High Redox Potential Laccase; High temperature; Humanities and Social Sciences; Kraft Lignin; Laccase; Laccase Activity; Lignin; multidisciplinary; Organic solvents; pH effects; Redox potential; Science; Science (multidisciplinary); Secretion; Site-directed mutagenesis; Surface Salt Bridges; Thermal stability; Surface Salt Bridges; Kraft Lignin; Laccase Activity; High Redox Potential Laccase; Cupredoxin Domains

The robustness of a high-redox potential laccase has been enhanced by swapping its second cupredoxin domain with that from another fungal laccase, which introduced a pool of neutral mutations in the protein sequence without affecting enzyme functionality. The new laccase showed outstanding stability...