Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2010 Mar;108(3):998-1006.
doi: 10.1111/j.1365-2672.2009.04505.x. Epub 2009 Jul 30.

Random mutants of a Pleurotus ostreatus laccase as new biocatalysts for industrial effluents bioremediation

Affiliations

Random mutants of a Pleurotus ostreatus laccase as new biocatalysts for industrial effluents bioremediation

A Miele et al. J Appl Microbiol. 2010 Mar.

Abstract

Aims: To select better performing laccase variants among the 2300 randomly mutated variants of Pleurotus ostreatus POXA1b laccase to develop improved laccase-based biocatalysts.

Methods and results: Screening of collections of 2300 randomly mutated variants of POXA1b was performed by assaying activity towards the phenolic substrate 2,6-dimethoxyphenol. Two new variants endowed with higher enzyme activity than the wild-type laccase were characterized, and their ability to decolourize industrial dyes with complex trisazo-, polyazo- and stilbene-type structures, in the absence of mediators, was demonstrated. One of the mutants (2L4A) was also proved to be highly stable at both acidic and alkaline pH values (displaying a half-life of around 1 month at the pH levels of both 5 and 10).

Conclusions: In comparison with the wild-type laccase, the new selected 2L4A mutant shows a significant increase in stability at acidic pH, whilst storing its high stability at alkaline pH. This variant also represents a more versatile enzyme with respect to both the variety of xenobiotics degraded and the operative conditions.

Significance and impact of the study: This work represents the first example of improvement of a basidiomycete laccase for industrial effluents bioremediation by directed evolution.

PubMed Disclaimer

References

    1. Aktaş, N. and Tanyolaç, A. (2003) Reaction conditions for laccase catalyzed polymerization of catechol. Bioresour Technol 87, 209-214.
    1. Alcalde, M., Ferrer, M., Plou, F.J. and Ballesteros, A. (2006) Environmental biocatalysis: from remediation with enzymes to novel green processes. Trends Biotechnol 24, 281-287.
    1. Alloway, B.J. and Ayres, D.C. (1998) Water, air, & soil pollution 102. In Chemical Principles of Environmental Pollution Vol. 102(1-2), pp. 216-218. London: Chapman & Hall/Blackie Academic.
    1. Baldrian, P. (2006) Fungal laccases: occurrence and properties. FEMS Microbiol Rev 30, 215-242.
    1. Bertrand, T., Jolivalt, C., Briozzo, P., Caminade, E., Joly, N., Madzak, C. and Mougin, C. (2002) Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry 41, 7325-7333.

Publication types