Cooperation of Fungal Laccase and Glucose 1-Oxidase in Transformation of Björkman Lignin and Some Phenolic Compounds

Leonowicz, Andrzej; Rogalski, Jerzy; Jaszek, Magdalena; Luterek, Jolanta; Wojtas-Wasilewska, M.; Malarczyk, Elżbieta; Ginalska, Grażyna; Fink-Boots, M.; Cho, Nam-Seok

doi:10.1515/hf.1999.062

Cited by 23 publications

(13 citation statements)

References 23 publications

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“…The copolymerization of tested laccase solutions resulted in higher durability of their activity on the surface unit [26] and relatively higher potential, which may be significant for its future usage in construction of electrochemical cathodes [36]. …”

Section: Resultsmentioning

confidence: 99%

Chemical Modifications of Laccase from White-Rot Basidiomycete Cerrena unicolor

Kucharzyk

Janusz

Karczmarczyk

et al. 2012

Appl Biochem Biotechnol

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Laccases belong to the group of phenol oxidizes and constitute one of the most promising classes of enzymes for future use in various fields. For industrial and biotechnological purposes, laccases were among the first enzymes providing larger-scale applications such as removal of polyphenols or conversion of toxic compounds. The wood-degrading basidiomycete Cerrena unicolor C-139, reported in this study, is one of the high-laccase producers. In order to facilitate novel and more efficient biocatalytic process applications, there is a need for laccases with improved biochemical properties, such as thermostability or stability in broad ranges of pH. In this work, modifications of laccase isoforms by hydrophobization, hydrophilization, and polymerization were performed. The hydrophobized and hydrophilized enzyme showed enhanced surface activity and higher ranges of pH and temperatures in comparison to its native form. However, performed modifications did not appear to noticeably alter enzyme’s native structure possibly due to the formation of coating by particles of saccharides around the molecule. Additionally, surface charge of modified laccase shifted towards the negative charge for the hydrophobized laccase forms. In all tested modifications, the size exclusion method led to average 80 % inhibition removal for hydrophilized samples after an hour of incubation with fluoride ions. Samples that were hydrophilized with lactose and cellobiose showed an additional 90 % reversibility of inhibition by fluoride ions after an hour of concluding the reaction and 40 % after 24 h. The hydrophobized laccase showed higher level of the reversibility after 1 h (above 80 %) and 24 h (above 70 %) incubation with fluoride ions. The addition of ascorbate to laccase solution before a fluoride spike resulted in more efficient reversibility of fluoride inhibitory effect in comparison to the treatments with reagents used in the reversed sequence.

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Section: Resultsmentioning

confidence: 99%

Chemical Modifications of Laccase from White-Rot Basidiomycete Cerrena unicolor

Kucharzyk

Janusz

Karczmarczyk

et al. 2012

Appl Biochem Biotechnol

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“…Among the Cerrena genus the most studied is Cerrena unicolor laccase -a glycoprotein (from 17 up to 24% carbohydrates) with a molecular weight in the range from 55 to 79 kDa [23 -28]. C. unicolor laccase was used in biodegradation and bioremediation [29,30], delignification [31], and decolorization [32 -34]. Furthermore, possible applications of the enzyme in amperometric biosensors were also reported [35 -38].…”

Section: Introductionmentioning

confidence: 99%

Comparative Spectroelectrochemical Studies of Lyophilized and Nonlyophilized Laccases from Cerrena unicolor Basidiomycete

et al. 2007

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The electrochemical, spectroelectrochemical, and kinetic investigations of two preparations of Cerrena unicolor laccase, lyophilized (LLAC) and nonlyophilized frozen enzymes (FLAC), were performed. It was found that the value of the redox potential of the T1 site of C. unicolor laccase is ca. 750 vs. NHE. It was also shown that one of the redox potentials of the T2/T3 cluster of C. unicolor laccase is close to 400 mV, as was previously confirmed for other blue multicopper oxidases, such as trees and fungal laccases, ascorbate oxidase, and bilirubin oxidase. Furthermore, the poor stability of both preparations, but especially of LLAC, in their reduced state was confirmed using mediated and mediatorless spectroelectrochemical studies. DET-based biocatalytic reduction of O 2 by C. unicolor laccase was only obtained, when FLAC was directly adsorbed on a spectrographic graphite electrode. Moreover, only low values of the steady-state potentials of gold and graphite electrodes modified by C. unicolor laccase were also found. Heterogeneity of the 3-D structures of laccase molecules, conformational changes, and partial denaturation of the enzyme, which appeared after enzyme isolation, purification, and especially lyophilization, were found to be the reasons for the low bioelectrocatalytic current, the high K M -value towards O 2 , and the unusual electrochemical behavior of C. unicolor laccase used in the present study. In spite of the comparable specific activity and long-term stability of both preparations in homogeneous solution, the stability of immobilized LLAC was found to be inadmissibly low for both fundamental studies and possible electrochemical applications. Indeed, FLAC is a much better source of enzyme than its lyophilized counterpart.

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“…Among others, these relate to levels of laccase, peroxidase, and phenol oxidase, which take part in the metabolism of phenolic compounds and in the degradation of lignin (Eriksson et al 1990;Hammel et al 1993;Leonowicz et al 1999). Phenolic substances are active in the process of building mushroom cell walls (Kitamoto et al 2000).…”

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confidence: 99%

Changes in phenol oxidases and superoxide dismutase during fruit-body formation of Pleurotus on sawdust culture

Cho

Malarczyk

et al. 2002

Mycoscience

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Ishikawa et al. 1983;Matsumoto 1988;Ohga 1992;.The fruiting process in higher fungi is connected with several biochemical changes. Among others, these relate to levels of laccase, peroxidase, and phenol oxidase, which take part in the metabolism of phenolic compounds and in the degradation of lignin (Eriksson et al. 1990;Hammel et al. 1993;Leonowicz et al. 1999). Phenolic substances are active in the process of building mushroom cell walls (Kitamoto et al. 2000). Phenols are very sensitive to the presence of active forms of oxygen and can be subject to various oxidative processes. Superoxide radicals are also able to initiate these processes, and it is known that autooxidation of diphenols decreases in the presence of superoxide dismutase (SOD) (Misra and Fridovich 1975). During enzymatic oxidation of diphenols, H 2 O 2 is also generated, becoming a good electron acceptor for peroxidase, and it activates enzyme change (Jiang and Miles 1993).The purpose of this article is to report on the changes in phenol oxidases [peroxidase, laccase, and Mn-dependent peroxidase (MnP)] and SOD, which take part in lignin metabolism, and on the level of phenols and free radical during the fruiting process.Two strains of Pleurotus species from the Fungi Collection of Cheongju (FCC) and the Fungi Collection of Lublin (FCL) were used; these were P. ostreatus (Jacq.: Fr.) Kummer (FCC-822) and P. sajor-caju (Fr.) Singer (FCL-215). The fungi were cultivated in polypropylene bags containing 1.5 kg of solid beech sawdust-wheat bran medium (80 : 20 w/w). The bags were incubated for 30 days at 25°C and moved to a conditioned room at 8°-15°C and 90% humidity for about 5-10 days for primordia formation. When the first primordia appeared, the culture bag was opened and moved to an illuminated room (about 500 lx) at 10°-15°C for 10 days for fruit-body growth. Samples were taken from cultures at various stages of development: mycelium before fruiting (Mbf) on the 30th day from inoculation, primordia (P) on the 35th day, small fruit-body (F1) on the 42th day, medium fruit-body (F2) on he 45th day, large mature fruit-body (F3) on the 50th day, and mycelium after fruiting (Maf) on the 60th day. Five liters of 50 mM Abstract Peroxidase and laccase activities increased rapidly up to the formation of primordia and then declined throughout the entire stage of fruiting. In the case of Pleurotus ostreatus, the level of Mn-dependent peroxidase was very low in primordia and fruiting stages but gradually increased with the growth of the fruit-body, whereas no activity was detected in Pleurotus sajor-caju during all growth stages. Superoxide dismutase activity was observed mainly at the fruiting stages. These results show that changes in concentration of lignin-related enzymes are associated with the fruiting process.Key words Fruit-body · Lignin-degrading enzymes · Phenol oxidase · Pleurotus · Superoxide dismutase Fruit-body development of mushrooms generally consists of two stages. One stage is primordia formation, which requires relatively lower temperat...

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Cooperation of Fungal Laccase and Glucose 1-Oxidase in Transformation of Björkman Lignin and Some Phenolic Compounds

Cited by 23 publications

References 23 publications

Chemical Modifications of Laccase from White-Rot Basidiomycete Cerrena unicolor

Chemical Modifications of Laccase from White-Rot Basidiomycete Cerrena unicolor

Comparative Spectroelectrochemical Studies of Lyophilized and Nonlyophilized Laccases from Cerrena unicolor Basidiomycete

Changes in phenol oxidases and superoxide dismutase during fruit-body formation of Pleurotus on sawdust culture

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