Palmieri G, Giardina P, Bianco C, Fontallella B, Sannina G. Copper induction of laccase isoenzyme in the lignolytic fungus Pleurotus ostreatus. Radical-based coupling or redox recycling of phenolic substrates acting as mediators broadens the spectrum of laccase substrates [28]. Assadi G., Vesterlund L., Bonfiglio F., Mazzurana L., Cordeddu L., Schepis D., Mjosberg J., Ruhrmann S., Fabbri A., Vukojevic V., et al. and A. ochraceus cells. Cu-oxidase_4 is a multicopper polyphenol oxidoreductase laccase. The enzyme moderates the sensitivity of E. coli to copper by exhibiting significant activity against siderophores utilized by E. coli for FeII uptake [130]. https://iopscience.iop.org/article/10.1088/1755-1315/406/1/012013 from 8600 Rockville Pike Many countries pose some rules and regulation for the pollutants which includes phenols and amines [115]. Bacterial (and plant) laccases belong to low-redox potential enzymes, with a redox potential at the T1 site (E0T1) below 460 mV vs. NHE [108,112,113]. Interestingly, aquatic fungal species were denied the ability to decompose lignin for many years. Effect of synthetic and natural culture media on laccase production by white rot fungi. This feature may contribute to the high stability of the enzyme [3]. Williamson PR. Junghanns C, Moeder M, Krauss G, Martin C, Schlosser D. Degradation of the xenoestrogen nonylphenol by aquatic fungi and their laccases. Such mediator-based oxidations occur principally in basidiomycetes, which are very efficient lignocellulose decomposers. Lac1 mutants with a disrupted lac gene (LAC1) are less pigmented, rarely produce conidia, and have reduced aerial mycelial mass and radial growth rates. Laccase producing bacterium, <i>Bacillus subtilis</i> MTCC 2414, was subjected to optimization by conventional techniques and was partially purified using ammonium salt precipitation method. With numerous organic and inorganic substrates, this enzyme is engaged in a variety of catalytic functions, which is generally described as protective against adverse environmental factors, including competitive or parasitic organisms and toxic compounds. Microbiol. and P. putida cultures [54,55]. In addition to their role in the digestibility and palatability of plant tissues, melanin formation increases the cell wall resistance to insects and pathogens attack [69]. [193], laccases in Heterobasidion annosum may act as a virulence factor during interactions with P. sylvestris seedlings [193]. Pseudomonas CopA shows limited but significant sequence homology with MCO proteins and is necessary for the expression of full copper resistance in these bacteria [132]. It has been found that 25C is the optimal temperature for laccase production in presence of light, but, in case of dark, the optimal temperature is 30C [19]. In 1883 Yoshida discovered that the first listed species in which laccase was detected was the Chinese lacquer tree Rhus vernicifera. Epub 2015 Oct 7. Besides solid wastes, wastewater from the food processing industry is particularly promising for that. Sugumaran M. Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Microbiol Res 2009,164(1):105-113. The structure and function of fungal laccases. The laccase from P. ostreatus is almost fully active in the temperature range of 40C60C, with maximum activity at 50C. Phenolic compounds are oxidized by laccase to phenoxyl radicals, which then engage in either coupling-based polymerization or radical rearrangement. S. ipomoea laccase retains 100% activity in 1 M NaCl at pH 8.0 [115]. The oval shapes represent blue-copper-binding sites. Depending on the redox potential, laccases are divided into two groups: low- and high-redox-potential enzymes. Andrews S.C., Robinson A.K., Rodriguez-Quinones F. Bacterial iron homeostasis. The https:// ensures that you are connecting to the Biotreatment of tannin-rich beer-factory wastewater with white-rot basidiomycete coriolopsis gallica monitored by pyrolysis/gas chromatography/mass spectrometry. Despite the low amino acid sequence homology between fungal and bacterial laccases, their molecular architecture is similar, and the overall geometry of their active sites is highly conserved [5,12,13]. Biochemical and molecular characterization of the diphenol oxidase of, Williamson P.R., Wakamatsu K., Ito S. Melanin biosynthesis in. Production of laccase by, Hess J, Leitner C, Galhaup C, et al. Sterjiades R., Dean J.F., Eriksson K.E. Aniszewski T., Lieberei R., Gulewicz K. Research on catecholases, laccases and cresolases in plants. The addition of inducer increases the concentration of a specific laccase enzyme [67]. Wang L, Tan Y, Sun S, Zhou L, Wu G, Shao Y, Wang M, Xin Z. Optimization and modeling of laccase production by, Heinzkill M, Bech L, Halkier T, Schneider P, Anke T. Characterization of laccases and peroxidases from wood-rotting fungi (family Coprinaceae), Lee IY, Jung KH, Lee CH, Park YH. Therefore, the spore pigments in Bacillus are responsible for its resistance against harsh conditions, and laccase is an effective enzyme in the synthesis of these spore pigments [119,127]. Minussi et al. In this Trametes versicolour is employed which decolorizes the synthetic dye, and for this purpose pulsed system has been developed [7377]. An official website of the United States government. Although there is undeniable evidence for prokaryotic protein glycosylation [110], glycosylation of bacterial MCOs has not been investigated extensively and there are only few reports related to the carbohydrate content of bacterial laccases [97,107,111]. Shevchenko S.M., Bailey G.W. Wei D.S., Houtman C.J., Kapich A.N., Hunt C.G., Cullen D., Hammel K.E. Recently it was found that brown-rot fungus Coniophora puteana [43] oxidizes the syringaldazine and supports the oxidation of ABTS in Laetiporus sulphureus [44]. Mayer A.M., Staples R.C. Laccase (lac) and manganese peroxidase (MnP) enzymes from the novel Klebsiella pneumoniae isolates, grown on lignin basic media (LBM) were purified by 80% ammonium sulphate fractionation, dialysis and DEAE-sepharose column chromatography. Crosslinked Enzyme Aggregates (CLEAs) of Laccases from Out of 59 isolates obtained from earthworm cast, seven were found positive for laccase production as they gave an intense reddish-brown colony on M162 agar plates containing 5 mM guaiacol (Figs. PMC legacy view For polyphenol oxidation, laccase has been used which is capable of removing the excess oxygen and also due to which the shelf life of beer increases [108, 109]. Laccase belongs to the blue multicopper oxidases and participates in cross-linking of monomers, degradation of polymers, and ring cleavage of aromatic compounds. Nakamura T. Purification and physico-chemical properties of laccase. However, only a few studies concerning cyanobacterial laccases have been reported [96,134]. A new basidiomycete, Trametes sp. Cloning and characterization of a new laccase from, Suzuki T., Endo K., Ito M., Tsujibo H., Miyamoto K., Inamori Y. It belongs to those enzymes, which have innate properties of reactive radical production, and its utilization in many fields has been ignored because of its unavailability in the commercial field. It is present in Ascomycetes, Deuteromycetes and Basidiomycetes and abundant in lignin-degrading white-rot fungi. Laccases are mainly monomeric, dimeric, and tetrameric glycoprotein. The well-known producers of prokaryotic laccase include gram-positive and gram-negative soil and aquatic bacteria belonging to the phyla - and -proteobacteria, Firmicutes, Cyanobacteria, Aquificae, and Deinococcus-Thermus, as well as members of Archaea (Table S1). Recently, it is also used in the design of biosensors, biofuel cells, as a medical diagnostics tool and bioremediation agent to clean up herbicides, pesticides and certain explosives in soil. Another well-known biological function of laccase in insects is production of melanin in the midgut as a primeval immune response against invasion of parasites [147], as described in D. melanogaster [210]. At room temperature or above, warming of beer can redissolve the complex. Learn more Principles of solid sate fermentation: Pandey A, Selvakumar P, Soccol CR, Nigam P. Solid state fermentation for the production of industrial enzymes. De Gregorio E., Spellman P.T., Rubin G.M., Lemaitre B. Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays. 2009). Laccase enzymes were first obtained from the cell sap of the Japanese lacquer tree. Ammonium sulphate is being commonly used for the enzyme purification for many years. Ligninolytic enzyme system of. Role of plant laccases in lignin polymerization. Laccase and beer storage. The number of laccase isoforms in different plant species varies. Detoxification of azo dyes by a novel pH-versatile, salt-resistant laccase from. Laccase from Stereum ostrea is purified with ammonium sulphate followed by Sephadex G-100 column chromatography with 70-fold purification [9]. Toward the functional analysis of uncultivable, symbiotic microorganisms in the termite gut. Laccase enzyme promotes cross linking of monomers, breakdown of polymers, and aromatic (phenolic) compounds. These two processes (sclerotization and pigmentation), known as cuticle tanning, involve the formation of covalent cross-links between polypeptides via oxidative and nucleophilic reactions of catechols and side-chain groups of amino acids. Laccases catalyze both anabolic and catabolic reactions. For improving the texture, volume, flavor and freshness of bread, wide range of enzymes are used. Laccase from LLP13 was first purified with column chromatography and then purified with gel filtration [10, 11]. Laccase treatment is more effective in comparison to conventional methods. But researchers have found much more efficient methodologies such as protein precipitation by ammonium sulphate, anion exchange chromatography, desalt/buffer exchange of protein, and gel filtration chromatography. Laccase production Laccase is an enzyme released in the extracellular medium by numerous fungi 12 through secondary . Liu L., Dean J.F., Friedman W.E., Eriksson K.E.L. Laccase: Enzyme revisited and function redefined. Laccase: properties and applications. Therefore, questions arise whether small fungal laccases are a missing link between bacterial 2dMCO and fungal 3dMCO or whether fungi evolved 2dMCO independently by losing one domain. 420, produced laccase in glucose medium and in cellobiose medium with induction by 0.5mM and 6mM o-toluidine [70]. As reported by Munk, Sitarz, Kalyani, Mikkelsen, and Meyer [29], fungal laccase can cleave bonds without the use of mediators in phenolic lignin model compounds. Hofrichter M., Fritsche W. Depolymerization of low rank coal by extracellular fungal enzyme systems.1. Viscosity of broth is the major problem associated with the fungal submerged fermentations. The enzyme was also isolated from leaves of Aesculus parviflora [143]. Received 2020 Jan 14; Accepted 2020 Jan 30. Cuticle sclerotization via laccase-mediated protein cross-linking processes was observed in the case of Manduca sexta and Tribolium castaneum [41]. MCOs encompass laccases (EC 1.10.3.2) and a large family of copper oxidases, which include, among others, ascorbate oxidases (EC 1.10.3.3), ceruloplasmin (EC 1.16.3.1), bilirubin oxidase (EC 1.3.3.5), phenoxazinone synthase (EC 1.10.3.4), and metallo-oxidase Fet3p (EC 1.16.3.1). Epub 2022 Jan 13. The production of laccase from bacterial source presents a cost-effective process for industrial applications as bacteria can produce the enzyme in a short duration and bacterial genes can be cloned and expressed in the host cell easily [20, 21].Bacterial laccases have already been characterized and reported for the removal of textile dyes, treatment of industrial effluents, pulp and paper . Bell A.A., Wheeler M.H. A developmentally regulated gene cluster involved in conidial pigment biosynthesis in. Other functions are most probably the result of specialization, International Journal of Molecular Sciences. The CotA structure has been elucidated with the use of comparative modeling. Hoegger P.J., Kilaru S., James T.Y., Thacker J.R., Kues U. Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences. This problem of production of enzyme can be improved by using polymeric substrates like cellulose . Parallel metatranscriptome analyses of host and symbiont gene expression in the gut of the termite. Thomas BR, Yonekura M, Morgan TD, Czapla TH, Hopkins TL, Kramer KJ. Laccases oxidizes catechols in the cuticle to their corresponding quinones, which catalyzes protein cross-linking reactions. Biochemical and kinetic characterization of laccase and manganese Yeast extract, peptone, urea, (NH4)2SO4, and NaNO3 are the commonly used nitrogen sources. Bacterial laccases have several unique properties . Structural and redox properties of the small laccase Ssl1 from. These enzymes are produced with both submerged and solid-state fermentation processes. Potential biological role of laccase from the sponge, Tartar A., Wheeler M.M., Zhou X., Coy M.R., Boucias D.G., Scharf M.E. Figure 2. pH optimization for laccase production by isolate SB1. A characteristic feature of plant laccases is the ability to oxidize the substrate without the help of mediators [146]. Next to fungi, it is believed that actinomycetes are potent producers of laccases in nature [107], and their SLACs are thought to represent key evolutionary intermediates of the three-domain MCOs [16]. The authors declare no conflicts of interest. Pyridine nucleotide-quinone reductase.2. Banerjee UC, Vohra RM. The ability to oxidize lignin precursors suggests involvement of plant laccases in the lignification of the plant cell wall [32,140,141,150,151]. Bioremediation: a novel approach to food waste management. The appearance of organisms is shown in the timeline on the left in milliom (mln) years. Gianfreda L, Xu F, Bollag JM. The optimal temperature of laccase production differs greatly from one bacterium to another. Laccase activity is proportional to the abundance of bacterial laccase-like genes in soil from subtropical arable land. Endophytes in Lignin Valorization: A Novel Approach. Voriskova J., Baldrian P. Fungal community on decomposing leaf litter undergoes rapid successional changes. Laccase 2 is the phenoloxidase gene required for beetle cuticle tanning. SSF is suitable for the production of enzymes by using natural substrates such as agricultural residues because they mimic the conditions under which the fungi grow naturally [8285]. The high alkaline pH optimum (8.5 and 9 for ABTS and DMP, respectively) was shown for several Streptomyces laccases [106,107,114], whereas the highest temperature optimum (85 C) was reported for McoP isolated form Pyrobaculum aerophilum [112] and T. thermophilus laccase (92 C) [94]. The laccase gene (LAC1) is essential for, Kuo H.C., Detry N., Choi J., Lee Y.H. official website and that any information you provide is encrypted Authors: Felsenstein J. These capabilities could be related to the competitiveness of Azospirillum sp. Now, after almost 140 years of research, it seems that this copper-containing protein with a number of unique catalytic properties is widely distributed across all kingdoms of life. The initial electron acceptor in laccase-catalyzed oxidation is copper T1 located in the cavity close to the enzyme surface [26]. [58] found that mycelia are damaged when fungus is grown in the stirred tank reactor and laccase production by Trametes multicolour is considerably decreased. Yeast Hosts for the Production of Recombinant Laccases: A Review. In Monochamus alternatus, laccase-2 plays a role in pupal pigmentation and sclerotization of adult cuticle [199]. Laccase production is triggered by nitrogen depletion but some nitrogen strains do not affect the enzyme activity . Laccase-like genes are identified in important human pathogens such as E. coli, Bordetella pertusis, P. aeruginosa, Campylobacter jejuni, Yersinia pestis, and Mycobacterium leprae [83]. Cryptococcus neoformans is Basidiomycetes yeast which produces laccase and oxidizes phenols and aminophenol but is unable to oxidize tyrosine [1]. The Eggert C. Laccase-catalyzed formation of cinnabarinic acid is responsible for antibacterial activity of. Laccase secretion is considered as one of the basic fungal responses to the presence of antagonistic conditions: other microorganisms, xenobiotics, metals, toxins, and biologically active compounds. The https:// ensures that you are connecting to the A review. For example, five laccases are expressed in the xylem of P. trichocarpa [141], eight laccases in the xylem tissues of P. taeda [32,140], and as many as 17 laccase genes in A. thaliana [144,145]. Jimnez M., Kameyama K., Maloy W.L., Tomita Y., Hearing V.J. Laccase are catalyzed in the mono-electronic oxidation of a substrate from the expenditure of molecular oxygen. An experiment was performed by Ahm in which he took 2 types of soil: in soil 1, both free and immobilized laccase remove 100% of 2,4-DCP (without regard of moisture content). [56] extracted laccase from Trametes versicolour which showed high enzyme activity at broad range of pH and temperature ranges but the optimum activity was found at pH 3.0 and 50C temperature. Enzymatic dimerization of penicillin X. Morozova OV, Shumakovich GP, Gorbacheva MA, Shleev SV, Yaropolov AI. Walker J.R., Ferrar P.H. In previous studies, most of the isolated ligninolytic bacteria could only produce two main ligninolytic enzymes, especially a combination of MnP and Lac enzyme production (Shi et al. Optimization of laccase production by. and A.P. In fungi, laccases appear more than the higher plants. Farnet AM, Criquet S, Tagger S, Gil G, Le Petit J. Purification, partial characterization, and reactivity with aromatic compounds of two laccases from Marasmius quercophilus strain 17. Laccases have been detected in representatives of Anacardiaceae and other higher plants, including Pinus taeda, Acer pseudoplatanus, Nicotiana tabacum, P. trichocarpa, Liridendron tulipifera, Lolium perenne, A. thaliana, Zea mays, Oryza sativa, Saccharum officinarum, Brassica napus, and Brachypodium distachyon (Table S1) [136]. The laccase activity is associated with the spore surface and is linked to the melanin-like polymer present in the cell wall or in the periplasm of the spore capsules. DAcunzo F., Galli C., Gentili P., Sergi F. Mechanistic and steric issues in the oxidation of phenolic and non-phenolic compounds by laccase or laccase-mediator systems. Martins L.O., Soares C.M., Pereira M.M., Teixeira M., Costa T., Jones G.H., Henriques A.O. Cellobiose increase laccase activity by profusing branch in certain Trametes species [68]. Developmental characterization, function and regulation of a Laccase2 encoding gene in the honey bee, apis mellifera (Hymenoptera, Apinae). Eggert C., Temp U., Dean J.F.D., Eriksson K.E.L. Accessibility PDF Isolation and characterization of Laccase producing bacteria from Jiang Q, Cui Z, Wei R, Nie K, Xu H, Liu L. Front Bioeng Biotechnol. Laccase from fruiting bodies is purified with ammonium sulphate precipitation with 4070% saturation and DEAE cellulose chromatography then 1.34 and 3.07 fold purification is obtained respectively [95]. Han MJ, Choi HT, Song HG. Interestingly, the human LACC1 gene shows no similarity to the other mammalian proteins, since it contains a C-terminal domain homologous to bacterial multicopper polyphenol oxidases (PO) and laccase [10]. All PPO enzymes have an overlapping substrate spectrum and lack monophenol hydroxylating activity [61]. Extracellular enzyme production by freshwater ascomycetes. In contrast, the normal enzyme activity was pH 10 at 40 C and pH 8 at 40 C were indicated for Bacillus cereus and P. parafulva respectively. 2016 Feb;58(2):93-116. doi: 10.1007/s12033-015-9910-1. Cuticular phenoloxidase from the silkworm, bombyx mori: properties, solubilization, and purification. Many agricultural wastes such as grape seeds, grape stalks, barley bran [91], cotton stalk, molasses waste water [92] and wheat bran [93] are also used as substrate for laccase production. Investigations on different and less polluting mediators such as natural mediators produced by laccase and also their modification by chemical means or protein engineering should be carried out to . A good strategy for this purpose is the production of laccase by SSF using agro- industrial wastes as a support-substrate. De Gonzalo G., Colpa D.I., Habib M.H.M., Fraaije M.W. The protective role is common for all taxonomic groups and, most likely, it is the primary role of laccases in all living organisms. The ePub format uses eBook readers, which have several "ease of reading" features Isolated bacteria, then, were fermented in the 500 mL flask and followed with laccase activity analysis with adding guaiacol as substrate and read using spectrophotometer, resulted in 64 U/L, 54 . They act on both phenolic and nonphenolic lignin-related compounds as well as highly recalcitrant environmental pollutants which help researchers to put them in various biotechnological applications. Grzegorz Janusz, Anna Pawlik, [], and Andrzej Paszczyski. Isolation, characterization and function of laccase from Trichoderma. Biochemical characterisation of the coexisting tyrosinase and laccase in the soil bacterium. Tsai H.F., Wheeler M.H., Chang Y.C., Kwon-Chung K.J. Almagro L., Ros L.G., Belchi-Navarro S., Bru R., Barcel A.R., Pedreo M. Class III peroxidases in plant defence reactions. Laccase produced from Trametes sp. Parkinson NM, Conyers CM, Keen JN, MacNicoll AD, Smith I, Weaver RJ. Numerous publications and reviews have been devoted to expression regulation of laccases ( Piscitelli et al., 2011 ; Janusz et al., 2013 ). Production of ligninolytic enzymes by newly isolated bacteria from palm Andersen SO, Peter MG, Roepstorff P. Cuticular sclerotization in insects. [77] found that bacteria S. maltophilia decolorizes some synthetic dyes (methylene blue, methyl green, toluidine blue, Congo red, methyl orange, and pink) as well as the industrial effluent. Niku-Paavola ML, Karhunen E, Salola P, Raunio V. Ligninolytic enzymes of the white-rot fungus. Received 2011 Jan 25; Revised 2011 Mar 30; Accepted 2011 Apr 16. Plant PPOs are predominantly located in the thylakoid membranes of chloroplasts, while the mammalian enzymes are usually present inside specialized melanocytes [63]. The 65 kDa CotA purified from an overproducing E. coli strain exhibits EPR spectra typical of the family of blue multicopper oxidases. All these issues will be approached through the biotechnological application of these enzymes (dye N. Dhull, M. Michael, P. Simran, V. R. Gokak and E. Venkatanagaraju *. Many Trichoderma species such as T. atroviride, T. harzianum [15], and T. longibrachiatum [16] are the sources of laccases. Khammuang S, Sarnthima R. Laccase activity from fresh fruiting bodies of, Domnguez A, Couto SR, Sanromn MA. Thomas B.R., Yonekura M., Morgan T.D., Czapla T.H., Hopkins T.L., Kramer K.J. The chemical structure of dyes provides a resistance to fading when exposed to light, water, and other chemicals. It was found that during seed storage and germination, the TT10 gene related to the formation of antimicrobial quinones participates in the creation of a barrier against pathogens in Arabidopsis [62]. Polyphenol oxidase as a biochemical seed defense mechanism. In this work, a thermo-tolerant halophilic Bacillus aquimaris AKRC02 was isolated from pulp and paper mill waste sludge for efficient laccase production. This study investigated the effects of bioaugmented ensiling with laccase and Pediococcus pentosaceus on the fermentation quality, nutritive value, enzymatic hydrolysis, and bacterial community of alfalfa. Isolated laccase occurs as a multimeric enzyme and its activity is correlated with production of a dark-brown pigment [85,86]. To understand the role of laccase in virulence of T. marneffei, single, double, triple, and quadruple deletions of genes encoding lacA, lacB, lacC, and pbrB laccases were obtained. Moreover, some fungal species, for example Pleurotus ostreatus, also produce laccases that are smaller than the typical 3dMCO and consist of only two domains [11]. Laccase belongs to polyphenol oxidases, which is a very wide family of copper-containing atoms in the center, which serves as the catalytic site. Spectroscopic and electronic structure studies of the trinuclear Cu cluster active site of the multicopper oxidase laccase: nature of its coordination unsaturation. Sitarz A.K., Mikkelsen J.D., Meyer A.S. Phenol oxidase, peroxidase and organic matter dynamics of soil. Authors Address: The presence of the enzyme in the resin ducts of Anacardiaceae indicates a defense function against herbivores, predators, and bacterial and fungal invasion [147]. 2008), Three-dimensional structure of cotA laccase, Three-dimensional structure of cotA laccase from B. subtilis : a The classical Greek-key, Structure of the two-domain laccase SLAC from Streptomyces coelicolor (PDB: 3CG8); monomers are, Various industrial applications of bacterial, Various industrial applications of bacterial laccase, MeSH Most of the information about fungal laccases originates from species belonging mainly to Basidiomycota and Ascomycota (Table S1). The contribution of melanin to microbial pathogenesis. Bacterial laccase; Biotechnological applications; Laccase-mediated system; Multi-copper oxidase; Phenolic compound; Response surface methodology. Bourbonnais R, Paice MG, Reid ID, Lanthier P, Yaguchi M. Lignin oxidation by laccase isozymes from, Hlker U, Dohse J, Hfer M. Extracellular laccases in ascomycetes, Velzquez-Cedeo MA, Farnet AM, Ferr E, Savoie JM. Laccase from T. versicolour is purified with Ion Exchange chromatography followed by gel filtration with specific activity of 101UmL1 and 34.8-fold purification [55]. Submerged and solid-state modes of fermentation are used intensely for the production of laccase. The variety of commercial and industrial application of laccases has attracted much attention towards the research addressing different aspects of the protein characterization, production and fit for purpose molecule. Iyer G, Chattoo BB. Harakava R. Genes encoding enzymes of the lignin biosynthesis pathway in Eucalyptus. Ribeiro DS, Henrique SMB, Oliveira LS, Macedo GA, Fleuri LF. They found that 3237% activity of Lac-II was inhibited in the presence of Sn, Ag, and Hg while 56% and 48% Lac-II activity was inhibited in the presence of Cr and W, respectively. A number of recent papers described the differential expression of laccases as a response to diverse environmental factors [17,18], which most likely require synthesis of laccases with different substrate specificity and kinetic properties [19,20]. Dittmer N.T., Gorman M.J., Kanost M.R. Rearrangement of the electron transport system has been suggested as a way in which the laccase-positive cells adapt to endogenous reactive quinones generated by laccases [102]. 2013;82:1-28. doi: 10.1016/B978-0-12-407679-2.00001-6. Rodrguez A, Falcn MA, Carnicero A, Perestelo F, De La Fuente G, Trojanowski J. Laccase activities of, Scherer M, Fischer R. Purification and characterization of laccase II of, Binz T, Canevascini G. Purification and partial characterization of the extracellular laccase from, Edens WA, Goins TQ, Dooley D, Henson JM. Therefore, research in this area is oriented towards the search for efficient production systems. Phenoloxidases from larval cuticle of the sheep blowfly, Li Q., Wang X., Korzhev M., Schroder H.C., Link T., Tahir M.N., Diehl-Seifert B., Muller W.E.
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