• Applied Biological Chemistry
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• v.47 no.3
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• pp.287-292
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• 2004

The optimum conditions for lignin peroxidase production were studied. Lignin peroxidase was produced almost exclusively in stationary culture with the optimum media composition of malt extract 1 g, yeast extract 0.4 g, glucose 0.4 g and distilled water 100 ml. Tween 80 at 0.005% concentration and veratryl alcohol at 0.4 mM were very effective inducers for lignin peroxidase production.

• Journal of Microbiology and Biotechnology
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• v.27 no.1
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• pp.179-188
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• 2017

White-rot basidiomycetes are the organisms that decompose lignin most efficiently, and Trametes villosa is a promising species for ligninolytic enzyme production. There are several publications on T. villosa applications for lignin degradation regarding the expression and secretion of laccase and manganese peroxidase (MnP) but no reports on the identification and characterization of lignin peroxidase (LiP), a relevant enzyme for the efficient breakdown of lignin. The object of this study was to identify and partially characterize, for the first time, gDNA, mRNA, and the corresponding lignin peroxidase (TvLiP) protein from T. villosa strain CCMB561 from the Brazilian semiarid region. The presence of ligninolytic enzymes produced by this strain grown in inducer media was qualitatively and quantitatively analyzed by spectrophotometry, qPCR, and dye fading using Remazol Brilliant Blue R. The spectrophotometric analysis showed that LiP activity was higher than that of MnP. The greatest LiP expression as measured by qPCR occurred on the $7^{th}$ day, and the ABSA medium (agar, sugarcane bagasse, and ammonium sulfate) was the best that favored LiP expression. The amplification of the TvLiP gene median region covering approximately 50% of the T. versicolor LPGIV gene (87% identity); the presence of Trp199, Leu115, Asp193, Trp199, and Ala203 in the translated amplicon of the T. villosa mRNA; and the close phylogenetic relationship between TvLiP and T. versicolor LiP all indicate that the target enzyme is a lignin peroxidase. Therefore, T. villosa CCMB561 has great potential for use as a LiP, MnP, and Lac producer for industrial applications.

• The Korean Journal of Mycology
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• v.40 no.2
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• pp.98-103
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• 2012

This study has been conducted to screen the decolorization of 4 aromatic synthetic dyes and production of ligninolytic enzymes by 4 white rot fungi such as Bjerkanderia adusta, Cerrena unicolor, Pleurotus pulmonarius and Abortiporus biennis. It was found that B. adusta, C. unicolor, and P. pulmonarius have the ability to efficiently decolorize congo red and moderately decolorized amaranth and orange G in solid and liquid culture media. However, the decolorization rate of 4 synthetic dyes by A. biennis was relatively low. The decolorization of congo red, amaranth, orange G were related to the growth rate of the fungal mycelia in the solid medium. But, the all fungi tested did not efficiently decolorize methylene blue in the liquid culture media. To investigate the production of ligninolytic enzymes in media containing aromatic compounds, fungi were cultured in 1% naphthalene supplemented potato dextrose broth medium. All fungi tested had the capability to produce laccase, lignin peroxidase and manganese peroxidase, and B. adusta was the best ligninolytic enzymes producing white rot fungus among other fungi tested.

• Forest Science and Technology
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• v.13 no.4
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• pp.158-163
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• 2017

We examined the activities of lignin-degrading enzymes of the mycelium of cauliflower mushroom (Sparassis latifolia). Three different strains of S. latifolia collected from several sites in Korea and one crossbred strain were cultured on potato dextrose broth (PDB) and Kirk's medium in order to study the activities of their ligninolytic enzymes. Mycelial growth reached maximum levels between 14 and 21 days after inoculation and pH increased by 0.12 units over 35 days. Laccase activity began increasing after 14 days on both types of media. Manganese peroxidase (MnP) activity followed a trend similar to that of laccase on Kirk's medium, but not on PDB. The activity of lignin peroxidase (LiP) differed from that of other enzymes; its activity decreased by half after 14 days on PDB but remained constant on Kirk's medium over 35 days. The total protein concentration increased considerably after 14 days and peaked at 21 days on PDB. A similar maximum was attained on Kirk's medium. In contrast, the residual glucose increased rapidly at 14 days on Kirk's medium, while increasing gradually up to 28 days on PDB. This study indicates that S. latifolia is more similar to white rot fungi than to other brown rot fungi.

• Journal of Mushroom
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• v.17 no.4
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• pp.247-254
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• 2019

Trametes hirsuta, a white rot fungus, exhibits the ability to degrade synthetic aromatic dyes such as congo red (CR), methylene blue (MB), crystal violet (CV), and remazol brilliant blue R (RBBR). The mycelia of T. hirsuta degraded RBBR and CR more efficiently than CV and MB in the PDB liquid medium (supplemented with 0.01% 4 aromatic dyes). In these mycelia the activities of three ligninolytic enzymes-laccase, manganese peroxidase (MnP), and lignin peroxidase (LiP)-were observed. Among these, laccase was identified to be the major enzyme responsible for the degradation of the four aromatic dyes. The degradation of bisphenol A was also investigated by culturing the mycelia of T. hirsuta in YMG medium supplemented with 100 ppm bisphenol A. The mycelia of T. hirsuta were found to degrade bisphenol A by 71.3, 95.3, and 100 % within incubation periods of 12, 24, and 36 hr, respectively. These mycelia also showed ligninolytic enzyme-like activities including those similar to laccase, MnP, and LiP. Therefore, these results indicate that T. hirsuta could emerge as a potential tool for the remediation of environmental contamination by aromatic dyes and bisphenol A.

• Journal of Microbiology
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• v.43 no.6
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• pp.555-560
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• 2005

Laccase is one of the ligninolytic enzymes of white rot fungus Trametes versicolor 951022, a strain first isolated in Korea. This laccase was purified 209-fold from culture fluid with a yield of $6.2\%$ using ethanol precipitation, DEAE-Sepharose, Phenyl-Sepharose, and Sephadex G-100 chromatography. T. versicolor 951022 excretes a single monomeric laccase showing a high specific activity of 91,443 U/mg for 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as a substrate. The enzyme has a molecular mass of approximately 97 kDa as determined by SDS-PAGE, which is larger than those of other laccases reported. It exhibits high enzyme activity over broad pH and temperature ranges with optimum activity at pH 3.0 and a temperature of $50^{\circ}C$. The $K_m$ value of the enzyme for substrate ABTS is $12.8{\mu}M$ and its corresponding $V_{max}$ value is 8125.4 U/mg. The specific activity and substrate affinity of this laccase are higher than those of other white rot fungi, therefore, it may be potentially useful for industrial purposes.

• Asian-Australasian Journal of Animal Sciences
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• v.23 no.5
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• pp.680-692
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• 2010

This paper gives an overview of the availability, nutritive quality, and possible strategies to improve the utilization of rice straw as a feed ingredient for ruminants. Approximately 80% of the rice in the world is grown by small-scale farmers in developing countries, including South East Asia. The large amount of rice straw as a by-product of the rice production is mainly used as a source of feed for ruminant livestock. Rice straw is rich in polysaccharides and has a high lignin and silica content, limiting voluntary intake and reducing degradability by ruminal microorganisms. Several methods to improve the utilization of rice straw by ruminants have been investigated in the past. However, some physical treatments are not practical because of the requirement for machinery or treatments are not economical feasible for the farmers. Chemical treatments, such as NaOH, $NH_3$ or urea, currently seem to be more practical for onfarm use. Alternative treatments to improve the nutritive value of rice straw are the use of ligninolytic fungi (white-rot fungi), with their extracellular ligninolytic enzymes, or specific enzymes degrading cellulose and/or hemicellulose. The use of fungi or enzyme treatments is expected to be a more practical and environmental-friendly approach for enhancing the nutritive value of rice straw and can be costeffective in the future. Using fungi and enzymes might be combined with the more classical chemical or physical treatments. However, available data on using fungi and enzymes for improving the quality of rice straw are relatively scarce.

• Journal of Microbiology and Biotechnology
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• v.19 no.11
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• pp.1421-1430
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• 2009

With an aim to evaluate dye decolorization by white rot fungus on natural living conditions, reproducing by solid-state fermentation, the process of triphenylmethane dyes decolorization using the white rot fungus P. ostreatus BP, cultivated on rice straw solid-state medium, has been demonstrated. Three typical dyes, including malachite green, bromophenol blue, and crystal violet, were almost completely decolorized by the fungus after 9 days of incubation. During the process of dye decolorization, the activities of enzyme secreted by the fungus, and the contents of soluble components, such as phenolic compounds, protein, and sugar, changed regularly. The fungus could produce ligninolytic, cellulolytic, and hemicellulolytic enzymes and laccase was the most dominant enzyme in solid-state medium. Laccase, laccase isoenzyme, and the laccase mediator could explain the decolorization of malachite green, bromophenol blue, and crystal violet by the fungus in solid-state medium, respectively. It is worth noting that the presence of the water-soluble phenolic compounds could stimulate the growth of fungus, enhance the production of laccase, and accelerate dye decolorization.

• Journal of the Korean Wood Science and Technology
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• v.21 no.3
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• pp.87-93
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• 1993

This study was undertaken to investigate the characteristics and the productivities of lignin olytic enzymes: laccase (Lac) and Mn-dependent peroxidase (MnP) from Coriolus versicolor and Lentinus edodes respectively. Enzymes were isolated from cultural filterates and purified according to the standard methods. These enzymes showed one band in SDS-PAGE and their molecular weights were found 62,000 and 45,000 dalton respectively. Polyclonal antibodies against Lac and MnP were raised against mouse. In the ELISA (enzyme-linked immunosorbent assay), Lac and MnP-antiserum produced a strong positive reaction with Lac and MnP antigen($A_{405}$=2.50 and 3.53 respectively). The sera to negative (S/N) ratio was determined by the dividing the mean absorbance of antibodies by the corresponding diluted samples from normal mouse serum. The sera produced showed 2 times more positive reaction in S/N ratio than negative sera.

• 한국생물공학회:학술대회논문집
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• 2002.04a
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• pp.473-476
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• 2002

A lignin degradation bacteria, symbiotic bacteria was isolated from the gut of Sympetrum depressiusculum and tested for its lignin degrading activity using lignin model compounds and related aromatic compounds. The strain was identified as Serratia marcescens HY-5 based on the 165 rDNA, cellular fatty acid composition, biochemical and physiological characteristics. S. marcescens showed 40-50% lignin degrading activity in the media that contained vaillin, guaiacol and dealkaline lignin. S. marcescens showed three ligninase activities [Jaccase, lignin peroxidase(LiP) and Manganase peroxidase(MnP)]. Addition of dealkaline lignin to the basal media increased about 6fold of laccase activity. Vanillic acid or vanillin increase 1.3fold of MnP activity and p-coumaric acid increased 12fold of LiP activity which added to the basal medium.