Laccase

From WikiMD's Food, Medicine & Wellness Encyclopedia

Cu3Im8laccase

Laccase is an enzyme belonging to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as the acceptor. Laccases catalyze the oxidation of a wide range of organic and inorganic substrates, including phenols, polyphenols, and anilines, by reducing molecular oxygen to water. These enzymes are widely distributed in plants, fungi, and microorganisms. In fungi, laccases play a crucial role in the degradation of lignin, a complex aromatic polymer abundant in wood, which is a critical process for carbon cycling in forest ecosystems. Additionally, laccases have applications in bioremediation, the food industry, textile processing, and as biosensors.

Structure and Mechanism[edit | edit source]

Laccases are multicopper oxidases; they contain four copper ions per molecule, divided into three types (T1, T2, and T3). The T1 copper site is where the substrate oxidation occurs, and the electrons are transferred from the substrate to the T2/T3 trinuclear copper cluster, where the reduction of oxygen to water takes place. The structure of laccases allows for the efficient reduction of oxygen, which is a relatively inert molecule, without the production of harmful reactive oxygen species.

Biological Function[edit | edit source]

In fungi, laccases are involved in several physiological processes, including pigment formation, plant pathogenesis, and especially the degradation of lignin. Lignin degradation is essential for the carbon cycle, as it enables the breakdown of plant biomass and the release of carbon dioxide back into the atmosphere. In plants, laccases are thought to be involved in the synthesis of lignin, among other functions.

Applications[edit | edit source]

Due to their broad substrate specificity and the ability to oxidize substrates in the presence of oxygen, laccases have been explored for various industrial applications:

- Bioremediation: Laccases can degrade a wide range of pollutants, including phenolic compounds, dyes, and plastics, making them useful for environmental cleanup. - Food industry: They are used in the production of beverages, such as wine and beer, to stabilize color and to remove undesired phenolic compounds. - Textile industry: Laccases are employed in the bleaching of textiles and the decolorization of textile dyes. - Biosensors: Due to their specificity, laccases can be used in biosensors for detecting phenols and other environmental pollutants.

Research and Development[edit | edit source]

Research on laccases has focused on improving their stability, oxidation potential, and substrate range through protein engineering and immobilization techniques. The discovery of new laccase-producing organisms and the cloning of laccase genes into high-yield expression systems are also areas of active research, aiming to produce laccases more efficiently and cost-effectively for industrial applications.

Challenges[edit | edit source]

One of the main challenges in the wider application of laccases is their relatively low stability under operational conditions and their need for mediators to oxidize non-phenolic substrates. Developing laccase-mediator systems that are both effective and environmentally friendly remains an area of ongoing research.

Laccase Resources
Doctor showing form.jpg
Wiki.png

Navigation: Wellness - Encyclopedia - Health topics - Disease Index‏‎ - Drugs - World Directory - Gray's Anatomy - Keto diet - Recipes

Search WikiMD


Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro) available.
Advertise on WikiMD

WikiMD is not a substitute for professional medical advice. See full disclaimer.

Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.


Contributors: Prab R. Tumpati, MD