Objective
White-rot fungi produce extra-cellular lignin-modifying enzymes, laccase, lignin peroxidases (LiPs) and manganese peroxidases (MnPs) in varying combinations. Laccase is a copper-containing oxidase which utilises molecular oxygen as oxidant and oxidises e.g. phenolic rings to phenoxy radicals. The efficiency and capacity of these enzymes to oxidise aromatic compounds are investigated to obtain fundamental knowledge which is needed to improve catalytical properties and facilitate genetic modification of these enzymes.
Research goals are: to produce and characterise laccase and other related oxidative enzymes of Phlebia radiata, Phlebia tremellosa, Panus tigrinus, Coriolus versicolor, Agaricus bisporus, Armillaria mellea and other related fungi; to study substrate specificities of laccases and oxidases from selected fungi; to clarify catalytic properties of the enzymes through detailed structural analysis of enzyme proteins.
Lignin-degrading activities of fungi are determined, e.g. by monitoring modification or degradation of lignin by spectrophotometry, by evolution of 14CO2 from 14C-labelled lignin and by assaying activities of laccase, LiPs and MnPs and the physiological factors affecting lignin degradation. Major forms of oxidases are purified using the methods already developed in the participating institutes, e.g. ion-exchange and gel-permeation chromatography. For the purification of minor isoenzyme forms, separation methods with high resolution capacity are adopted. Characterisation of oxidases includes the determination of molecular masses and sub-units content of purified oxidases, pI, pH-optimum, temperature stability etc. Catalytical properties of oxidases are studied, e.g. range of monomeric aromatic substrates with different substituents in different positions oxidised by oxidases. Reactions of oxidases with dimeric model compounds of lignin are investigated and products from these reactions are determined (e.g. HPLC, GC-MS etc). Reactions of oxidases with polymeric lignins from different sources, with different content of monomers and after different chemical treatment (industrial lignins) are investigated. Molecular properties of oxidases, e.g. copper contents in enzymes are determined. Spectral analysis is carried out (absorption spectra, EPR-spectra).
Expected results will give relevant know-how to help to choose the right oxidase or laccase for a certain application, e.g. on the catalytic efficiency and molecular properties of laccases from three different types of fungi concerning which laccases are the most powerful oxidants and thus the most useful for applications, e.g. in pulp and paper industry to decrease energy and chemical consumption and in processes to remove environmental pollutants from soil and water.
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Coordinator
00014 Helsinki
Finland
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