title: Comparison of different microbial laccases as tools for industrial uses.
abstract: Laccases from different sources are employed in a number of biotechnological processes, each characterized by specific reaction constraints and thus requiring an enzyme with suitable properties. In order to avoid the bias generated by different assay methodologies, in this work we investigated the main properties of ten laccases from fungi and bacteria under identical conditions. As a general rule, the optimal activity was apparent at pH 3-4 and was lost at pH≥7.0 (all laccases were stable at pH≥7.0); enzymes active at neutral pH values were also identified. For all tested laccases, activity increased with temperature up to 80°C and stability was good at 25°C. Interestingly, laccases insensitive to high salt concentration were identified, this favoring their use in treating waste waters. Indeed, bacterial laccases retained a significant activity in the presence of DMSO (up to 40% final concentration) and of surfactants, suggesting that they can be applied in lignin degradation processes requiring solvents. The available laccases are versatile and satisfy requirements related to different processes. Notably, the recombinant laccase from Bacillus licheniformis favorably compares with the tested enzymes, indicating that it is well suited for different biotechnological applications.
authors: Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, via J.H. Dunant 3, 21100 Varese, Italy.
authors: Fabio
authors: F
authors: Tonin
authors: Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, via J.H. Dunant 3, 21100 Varese, Italy.
authors: Roberta
authors: R
authors: Melis
authors: ASA Spezialenzyme GmbH, Am Exer 19c, D-38302 Wolfenbüttel, Germany.
authors: Arno
authors: A
authors: Cordes
authors: Department of Genetics and Microbiology, University of Murcia, Murcia, Spain.
authors: Antonio
authors: A
authors: Sanchez-Amat
authors: Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory, Centro Interuniversitario di Biotecnologie Proteiche, Politecnico di Milano and Università degli Studi dell'Insubria, Milano, Italy. Electronic address: loredano.pollegioni@uninsubria.it.
authors: Loredano
authors: L
authors: Pollegioni
authors: Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory, Centro Interuniversitario di Biotecnologie Proteiche, Politecnico di Milano and Università degli Studi dell'Insubria, Milano, Italy.
authors: Elena
authors: E
authors: Rosini
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D052160:Benzothiazoles / Q000737:chemistry; D004121:Dimethyl Sulfoxide / Q000494:pharmacology; D005658:Fungi / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007218:Industrial Microbiology; D007700:Kinetics; D042845:Laccase / Q000302:isolation & purification / Q000378:metabolism*; D011136:Polysorbates / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013451:Sulfonic Acids / Q000737:chemistry; D013696:Temperature
chemical_list: D052160:Benzothiazoles; D011136:Polysorbates; D013451:Sulfonic Acids; C002502:2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid; D012965:Sodium Chloride; D042845:Laccase; D004121:Dimethyl Sulfoxide