Journal article

Authors list: Ruiz-Duenas, FJ; Aguilar, A; Martinez, MJ; Zorn, H; Martinez, AT

Publication year: 2007

Pages: 276-285

Journal: Biocatalysis and Biotransformation

Volume number: 25

Issue number: 2-4

ISSN: 1024-2422

DOI Link: https://doi.org/10.1080/10242420701422740

Publisher: Taylor and Francis Group

Abstract: 
The gene of a peroxidase described as being involved in carotenoid degradation was cloned from a strain that was conserved as Lepista irina (CBS 458.79). Gene sequencing revealed high nucleotide and amino-acid identity with Pleurotus eryngii gene vpl, which encodes a versatile peroxidase with unique catalytic properties, and only reported in Pleurotus and Bjerkandera species. Re-identification of the supposed L. irina strain revealed that, in fact, it is a P. eryngii strain. The new P. eryngii peroxidase was expressed in Escherichia coli, and the recombinant protein folded in the presence of cofactor to obtain the active form. The purified enzyme was able to oxidize Mn2+, veratryl alcohol, substituted phenols, and both low and high redox-potential dyes, demonstrating that it belongs to the versatile peroxidase family ( named VPL3). These catalytic properties agreed with the presence of both Mn2+ and aromatic-substrate oxidation sites in its molecular structure.

Harvard Citation style: Ruiz-Duenas, F., Aguilar, A., Martinez, M., Zorn, H. and Martinez, A. (2007) Gene cloning, heterologous expression, in vitro reconstitution and catalytic properties of a versatile peroxidase, Biocatalysis and Biotransformation, 25(2-4), pp. 276-285. https://doi.org/10.1080/10242420701422740

APA Citation style: Ruiz-Duenas, F., Aguilar, A., Martinez, M., Zorn, H., & Martinez, A. (2007). Gene cloning, heterologous expression, in vitro reconstitution and catalytic properties of a versatile peroxidase. Biocatalysis and Biotransformation. 25(2-4), 276-285. https://doi.org/10.1080/10242420701422740