Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species-Reference-Cited by-同舟云学术

Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species

Published:2021-02-26 Issue:3 Volume:14 Page:1026-1043
ISSN:1751-7915
Container-title:Microbial Biotechnology
language:en
Short-container-title:Microb. Biotechnol.

Author:

Olmeda Isidoro¹^ORCID,Casino Patricia²³⁴^ORCID,Collins Robert E.⁵⁶^ORCID,Sendra Ramón²^ORCID,Callejón Sara¹^ORCID,Huesa Juanjo²^ORCID,Soares Alexei S.⁷^ORCID,Ferrer Sergi¹^ORCID,Pardo Isabel¹⁸^ORCID

Affiliation:

1. ENOLAB Institut de Biotecnologia i Biomedicina (BioTecMed) Universitat de València Valencia Spain

2. Departament de Bioquímica i Biologia Molecular Universitat de València Valencia Spain

3. Institut de Biotecnologia i Biomedicina (BioTecMed) Universitat de València Valencia Spain

4. Group 739 of the Centro de Investigación Biomédica en Red sobre Enfermedades Raras (CIBERER) del Instituto de Salud Carlos III Valencia Spain

5. Office of Educational Programs Brookhaven National Laboratory Upton NY11973USA

6. Department of Chemistry and Physical Sciences Quinnipiac University Hamden CT06518USA

7. Photon Sciences Directorate Brookhaven National Laboratory Upton NY11973USA

8. Departament de Microbiologia i Ecologia Universitat de València Valencia Spain

Publisher

Wiley

Subject

Applied Microbiology and Biotechnology,Biochemistry,Bioengineering,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/1751-7915.13751

Reference75 articles.

1. A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye

2. Laccases are widespread in bacteria

3. Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure

4. Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp

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