期刊
JOURNAL OF APPLIED MICROBIOLOGY
卷 108, 期 3, 页码 998-1006出版社
WILEY
DOI: 10.1111/j.1365-2672.2009.04505.x
关键词
bioremediation; dye degradation; enzyme stability; phenol oxidase; random mutagenesis
资金
- Ministero dell'Universita e della Ricerca Scientifica (Progetti di Rilevante Interesse Nazionale, PRIN)
- Ministero Degli Affari Esteri di Intesa con il Ministero dell'Universita e della Ricerca
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.
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