Mode of Action, Properties, Production, and Application of Laccase: A Review

Abstract

Background and Source: Laccase belongs to the blue multi-copper oxidases, which are widely distributed in fungi and higher plants. It is present in Ascomycetes, Deuteromycetes, and Basidiomycetes and found abundantly in white-rot fungi. </P><P> Applications: Laccase enzymes because of their potential have acquired more importance and application in the area of textile, pulp and paper, and food industry. Recently, it is being used in developing biosensors for detection and removal of toxic pollutants, designing of biofuel cells and medical diagnostics tool. Laccase is also being used as a bioremediation agent as they have been found potent enough in cleaning up herbicides pesticides and certain explosives in soil. Because of having the ability to oxidize phenolic, non-phenolic lignin-related compounds and highly fractious environmental pollutants, laccases have drawn the attention of researchers in the last few decades. Commercially, laccases have been used to determine the difference between codeine and morphine, produce ethanol and are also being employed in de-lignify woody tissues. We have revised patents related to applicability of laccases. We have revised all the patents related to its wide applicability. </P><P> Conclusion: For fulfillment of these wide applications, one of the major concerns is to develop a system for efficient production of these enzymes at a broad scale. Research in the field of laccases has been accelerated because of its wide diversity, utility, and enzymology. This paper deals with recent trends in implementation of the laccases in all practical possibilities with the help of optimizing various parameters and techniques which are responsible for mass production of the enzyme in industries.

Dissecting the Polyhydroxyalkanoate-Binding Domain of the PhaF Phasin: Rational Design of a Minimized Affinity Tag

“…To validate MinP as an affinity tag, two enzymes, the ␤-galactosidase and the CueO oxidase from Escherichia coli, were genetically fused to minP by using the designed plasmid pSMinPN. Both enzymes are of wide applicability in the food industry for manufacturing lactosehydrolyzed products and the production of galactosylated products, in the case of the ␤-galactosidase (35), and for the textile and paper industries as well as for organic compound degradation with CueO oxidase (15,36). The ␤-galactosidase-coding gene was introduced by conventional cloning into XhoI and BamHI sites, resulting in the pSMinP-2 plasmid, and the cueO gene into XhoI and HindIII sites, resulting in the plasmid pSMinP-3.…”

Laccases: structure, function, and potential application in water bioremediation

“…A recent review of patents related to laccase applicability can be consulted in Ref. [188]. One strategy to overcome the limitations of mesophilic proteins is to search for those with desired properties, usually focusing on samples from extreme environments.…”

Probing the Role of the Conserved Arg174 in Formate Dehydrogenase by Chemical Modification and Site-Directed Mutagenesis

“…The specificity of the reaction can be evaluated by the ability of native enzyme’s ligands (e.g., substrate, inhibitor) to influence (promote or inhibit) the rate of inactivation [ 34 , 44 , 45 , 46 , 47 ]. In the present work, the effect of the substrates, formate, NAD + and NADH on the reaction of AMPS-HDB with CoFDH was investigated ( Figure 5 ).…”

“…Previously published works have established that Arg residues in proteins contribute significantly to protein stability through the formation of strong electrostatic interactions [ 44 , 45 ]. In particular, the guanidinium group of Arg enables the formation of electrostatic interactions in three possible directions, which allows the development of a larger number of electrostatic interactions [ 44 , 45 , 46 , 47 ]. The relative high pK a of the guanidinium group in Arg residues (~12.5) contributes to the formation of more stable and stronger electrostatic interactions, compared to that formed by Lys or His residues.…”