Laccases applications

Widsten P, Kandelbauer A. (2008). Laccase applications in the forest products industry a review. Enzyme Microb Technol, 42, 292-201. ... 

Couto SR, Herrera JTT. 2006. Industrial and biotechnological applications of laccases A review. Biotechnol Adv 24 500-513. 

Although the use of mediator compounds is scarcely applicable in deca-BDE in situ bioremediation processes, it is important to consider whether their presence enhances the degradation of the pollutant by the enzyme laccase because it is known that the fungus is able to produce naturally certain compounds that can act as mediators in pollutant degradation by laccase and this study would show the extent of their effect on deca-BDE degradation in case that laccase was involved. 

The laccases, classed as polyphenol oxidases, catalyze the oxidation of diphenols, polyamines, as well as some inorganic ions, coupled to the four-electron reduction of oxygen to water see Fig. 12.4 for the proposed catalytic cycle. Due to this broad specificity, and the recognition that this specificity can be extended by the use of redox mediators [27], laccases show promise in a range of applications [28], from biosensors [29-32], biobleaching [27, 33-35] or biodegradation [36], to biocatalytic fuel cells [1-3, 18, 26, 37-42]. 

Several applications of laccase have been reported in recent years (Rodrfguez-Couto and Toca-Herrera 2006). As shown in this section, many of these applications are similar to those published for peroxidase enzyme. 

The production and synthesis of polymers and medical agents is one of the most interesting potential uses for laccases in synthetic chemistry, where their application has been proposed for oxidative deprotection and the production of complex polymers and pharmaceutical agents. 

The cosmetic world has not been indifferent to the application of laccase for example, laccase-based hair dyes are less irritating and easier to handle than current hair dyes, because laccases replace H2O2 as an oxidizing agent in the dye formulation (Rodriguez-Couto and Toca-Herrera 2006). 

Duran N, Rosa MA, D Annibale A and Gianfreda L. 2002. Applications of laccases and tyrosinases (phe-noloxidases) immobilized on different supports a review. Enzyme Microb Technol 31 907-931. 

Minussi RC, Pastore GM and Durany N. 2002. Potential applications of laccase in the food industry. Trends Food Sci Technol 13 205-216. 

Morozova OV, Shumakovich GP, Shleev SV and Yaropolov YI. 2007. Laccase-mediator systems and their applications a review. Appl Biochem Microbiol 43(5) 523-535. 

Call FIP, Mucke I (1997) Minireview history, overview and applications of mediated ligni-nolytic systems, especially laccase-mediator-systems (Lignozym-Process). J Biotechnol 53 163-202... 

Jiang-Ping L, Wei L, Li-Ming X, Pei-Lin C (2001) Production of laccase by Coriolus versicolor and its application in decolorization of dyestuffs. I. Production of laccase by batch and repeated-batch processes. J Environ Sci 15 1—4... 

The biotechnological potential of laccases—working with air and producing water as sole by-product—has led to applications from the textile to the pulp and paper industries, from food applications to bioremediation, as well as their use in organic synthesis. 

It should be noted that some commercial enzyme preparations may contain several enzyme isomers (enzymes derived from one source which belong to the same enzyme class but differ in specificity, stability or other properties). This is most often the case when the commercial preparation was developed for a process industry application rather than a specific chemical biotransformation application. Some fungal enzymes, such as laccase, are sometimes supplied as crude enzyme mixtures. Fungal laccases are manufactured on a huge scale (multitonne per annum) and are principally used in bulk processes such as wood... 

For example, the small scale of the device was intended as a demonstration of architecture suitable for implanted applications. Mano et al. demonstrated a miniature fuel cell with bilirubin oxidase at the cathode catalyst that is more active at pH 7 and tolerates higher halide concentrations than does laccase. Additionally, the long-side-chain poly-(vinylpyridine)—Os(dialkyl-bis-imidazole)3 redox polymer discussed above was employed to both lower the anode potential and, via the long side chains, enhance electron transport from the biocatalyst. The cell achieved a current density of 830 at 0.52 V... 

Figu re 3.3 Conceptual process model for application of a coupled tyrosinase-laccase reaction converting tyrosol. Immobilized enzymes are first characterized with respect to substrate conversion rates, using tyrosol and hydroxytyrosol as substrates for tyrosinase and laccase, respectively. One hundred percent conversion can be achieved in Reactor 1 by use of sufficient tyrosinase... 

The produchon of oxidase enzymes in native strains is often not constitutive, since these enzymes are only required under specific conditions, such as nutrient stress. This imposes limitations on their application in continuous bioprocesses and one way of dealing with this issue is to develop improved expression systems. Laccase from Trametes sp. C30, which in its native strain is inducible and only weakly expressed, has been cloned and expressed in yeast to provide a functional recombinant enzyme with the same high activity and low redox potential as the native enzyme [68]. 

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