Abstract
There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society’s increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.
Highlights
Laccases (p–benzenediol: oxygen oxidoreductase EC 1.10.3.2) are multicopper-containing oxidases that are able to oxidize a wide range of phenol compounds and amines
Research should be focused on reducing the production cost and on developing the tools to better control the reaction on selected polyphenols and other substrates to be treated by these enzymes
The major challenges concerning the industrial use of laccases include the production costs, and the broad substrate specificity of laccases
Summary
Laccases (p–benzenediol: oxygen oxidoreductase EC 1.10.3.2) are multicopper-containing oxidases that are able to oxidize a wide range of phenol compounds and amines. O–O bond and the release results in the formation of a peroxide intermediate that is bound between one of the T3 copper ions of one water molecule, while the enzyme returns to the fully oxidized state (native intermediate, NI). The redox potential of a given laccase usually can determine the substrate range that the enzyme is able to oxidize. The non–phenolic parts of lignin have redox potentials up to 1.5 V, and cannot be oxidized by laccases This recalcitrant part of lignin can still be oxidized by laccases with the use of suitable mediators, which are small molecules that are first oxidized by laccases to radicals; they attack the substrate through different mechanisms, such as electron or radical hydrogen atom transfer [37]. LMS has been used for the oxidative synthesis of platform chemicals [45]
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