The culture conditions for maximum secretion of laccase by Loweporus lividus MTCC-1178 have been optimized. The laccase from the culture filtrate of L. lividus MTCC-1178 has been purified to homogeneity. The molecular weight of the purified laccase is 64.8 kDa. The enzymatic characteristics like K(m), pH, and temperature optimum using 2,6-dimethoxyphenol have been determined and found to be 480 microM, 5.0, and 60 degrees C, respectively. The K(m) values for other substrates like catechol, m-cresol, pyrogallol, and syringaldazine have also been determined and found to be 230, 210, 320, and 350 microM, respectively.

A laccase has been purified from the liquid culture growth medium containing bagasse particles of Fomes durissimus. The method involved concentration of the culture filtrate by ultrafiltration and anion exchange chromatography on diethyl aminoethyl cellulose. The sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and native polyacrylamide gel electrophoresis both gave single protein band indicating that the enzyme preparation was pure. The molecular mass of the purified laccase determined from SDS-PAGE analysis was 75 kDa. Using 2,6-dimethoxyphenol as the substrate, the determined K (m) and k (cat) values of the laccase are 182 μM and 0.35 s(-1), respectively, giving a k (cat)/K (m) value of 1.92 × 10(3) M(-1) s(-1). The pH and temperature optimum were 4.0 and 35 °C, respectively. The purified laccase has yellow colour and does not show absorption band around 610 nm found in blue laccases. Moreover, it transformed methylbenzene to benzaldehyde in the absence of mediator molecules, property exhibited by yellow laccases.

Laccases benzenediol: oxygen oxidoreductase (EC1.10.3.2), multicopper containing oxidoreductase enzymes, are able to catalyze the oxidation of various low-molecular weight compounds, specifically, phenols and anilines, while concomitantly reducing molecular oxygen to water. Because of their high stability, selectivity for phenolic substructures, and mild reaction conditions, laccases are attractive for fine chemical synthesis. This manuscript provides a discussion of the recent applications of this interesting enzyme in synthetic chemistry, including laccase and laccase-mediator catalyzed reactions. There for fungal laccases are consider as a perfect green catalysts is a prominent biotechnological applications. Thus laccases find potential applications in bleaching of paper pulp, biofuel cells and organic synthesis. They can perform transformations from the oxidation of functional group to the hetero nuclear coupling product of new antibiotics derivative.

Laccases belongs to multinuclear copper containing oxidase and can act as a variety of aromatic and non-aromatic compounds. Due to their broad substrate specificity, they are considered as a promising candidate in various industrial and biotechnological sectors. They are regarded as a green catalyst in biotechnology. The present review focuses on structure, reaction mechanism, categories, applications, economic feasibility, limitations, and future prospects of fungal laccases. Thus, this review would help in understanding laccases along with the areas, whichhas not been focused and requires attention. Since past, immense work has been carried out on laccases: yet, new discoveries and application are ever increasing which includes biofuel, biosensor, fiber board synthesis, bioremediation, clinical, textile industry, food, cosmetics, and many more.