• Journal of the Korean Society of Food Science and Nutrition
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• v.44 no.12
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• pp.1793-1798
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• 2015

Antioxidant activities of various solvent extracts from Coriolus versicolor were investigated for their total polyphenol content, total flavonoid content, 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) cation radical scavenging activity. C. versicolor extracts were produced by organic solvents such as ethanol, ethyl acetate, and methanol. Total polyphenol and flavonoid contents in the ethanol and ethyl acetate extracts were higher than those in the methanol extract. DPPH radical scavenging activity of methanol extract showed the highest value of 80.3%, which was similar to that of ascorbic acid (85.5%). All extracts showed good (>90.0%) ABTS cation radical scavenging activity. The antimicrobial activities of these extracts from C. versicolor were evaluated against six strains of bacteria using the disc diffusion method. All extracts showed antimicrobial activities against all tested bacteria except Staphylococcus aureus. These results indicate that various extracts from C. versicolor could be useful as natural antioxidant and antimicrobial agents.

• The Korean Journal of Mycology
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• v.15 no.2
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• pp.99-170
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• 1987

The production and properties of laccase(E.C.1.10.3.2) from Coriolus versicolor were studied. The results were as follows; The nutritional optimum conditions for laccase production were 1% indulin At, 0.3% peptone 0.1% $KH_2PO_4$, 0.02% $MgSO_4$, 0.1 mg% $CuSO_4$.and 0.005 mg% thiamine HCI. The optimum temperature and pH of laccase production were $25^{\circ}C$ and 5.0, and respectively, and the cultural period was 20 days. The optimum pH and temperature for the activity were 4.6 and $40^{\circ}C$, respectively. The enzyme was almost stable under the temperature of $40^{\circ}C$ and within the pH range of 4.0-5.0. The enzyme was stable at $40^{\circ}C$ for 30 min. $Cu^{++}$, $Fe^{++}$ and $Ca^{++}$ activated the enzyme activity, but $Mn^{++}$ and $Hg^{++}$ were inhibited. The enzyme was totally inhibited by 1 mM sodium azide and 1 mM potassium cyanide, and partly inhibited by EDTA and hydroxyamine.

• Biomolecules & Therapeutics
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• v.19 no.4
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• pp.438-444
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• 2011

The mushroom Coriolus versicolor contains biologically active polysaccharides, most of which belong to the ${\beta}$-glucan group. Diverse physicochemical properties, due to different sources and isolated types of ${\beta}$-glucans, can induce distinct biological activities. We investigated the effects of ${\beta}$-glucans from C. versicolor on phagocytic activity, nitric oxide (NO), TNF-${\alpha}$ production, and signaling of dectin-1, a well-known ${\beta}$-glucan receptor, in macrophages. ${\beta}$-Glucans increased phagocytic activity and TNF-${\alpha}$ and NO-iNOS/eNOS production. Laminarin, a specific inhibitor of dectin-1, showed strong inhibitory effects on phagocytosis and subsequent TNF-${\alpha}$, iNOS, and eNOS production increased by ${\beta}$-glucans, indicating that ${\beta}$-glucans reacts with dectin-1 receptors. We examined whether the aforementioned cytokines were involved in the signaling pathway from the dectin-1 receptor to phagocytosis, and found that the inhibition of iNOS, eNOS, and TNF-${\alpha}$ receptors significantly decreased ${\beta}$-glucan-induced phagocytosis. In conclusion, our study showed that dectin-1 signaling, triggered by ${\beta}$-glucans, subsequently elicited TNF-${\alpha}$ and NO-iNOS/eNOS production, and that these molecules seem to act as secondary molecules that cause eventual phagocytosis by macrophages. These findings suggest that C. versicolor could be used as a nutritional medicine that may be useful in the treatment of infectious disease.

• Microbiology and Biotechnology Letters
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• v.10 no.3
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• pp.191-196
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• 1982

In order to prevent the losses of the rice by fungal deterioration during storage, fungal contaminants were isolated and identified from the grain samples (Milyang Nr.23) stored for seven months from December, 1978 to June, 1979 in silo, flat store and Tongari. Out of thirty cultures isolated from Korean paddy and brown rice samples, twenty seven species were identified, and there are eleven species of Aspergillus (A. caespitosus, A. condidus, A. chevalieri, A fischeri, A. fumigatus, A. flavus, A. nidulans, A. oryzae, A. ruber, A. sydowii, A. versicolor), five species of Penicillium (P. atramentosum, p. chrysogenum, P. cyaneofulvum, P. nototum, P. steckii), two species of each Alternaria (Al. faesiculata, Al. grisea) and Curvalaria (C, interseminata, C. tetromea), and one species of each Trichothecium roseum, Nigrospora sphaerica, Rhizopus nigricans, Fusarium spp., Mucor spp., Helminthosporium spp., and Gliocladiopsis spp. The major types of fungi grown on the surface of paddy during storage were A. flavus and A. candidus, while A. ruber and A. sydowii appeared in brown rice samples. And also A. candidus, A. versicolor and A. glacus groups were considered as major deteriorating microorganisms in stored brown and paddy rice in Korea.

• Journal of the Korean Wood Science and Technology
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• v.20 no.4
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• pp.49-56
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• 1992

Seven white rot fungi (Irpex lactenis, Coriolus hirsutus, Lopharia mirabilis, Schizopora paradoxa, Ganoderma lucidum, Pleurotus ostreatus and Pycnoporus coccineus) native to Korea and two famous exotic lignin degradable white rot fungi (Coriolus versicolor and Phanerochaete chrysosporium) were investigated to clarify their physiological and physicochemical characteristics on white-rotted wood blocks. G. lucidum degraded wood blocks more seriously than those by exotic lignin-degrading fungi, C. versicolor and P. chrysosporium, but only slightly decreasecl the strength of wood which was compared to the weight loss, persumably on the account of its small use of cellulose when attacking wood. It is quite interesting to note that the holocellulose degradation rate of G. lucidum was also higher than any of the other tested fungi. The order of fungi, according to the lignin-decomposing rates, was G. lucidum>P. coccineus>C. versicolor>S. paradoxa>P. chrysosporium>L. mirabilis>P. ostreatus>C. hirsutus>I. lactenis. The lignin degradation of G. lucidum and P. coccineus which were collected in Korea was greater than that of C. versicolor and P. chrysosporium. If holocellulose degradation is not considered. G. lcidum has the merit of actual application in biomass conversion due to linin removal.

• Journal of the Korean Wood Science and Technology
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• v.29 no.3
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• pp.112-122
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• 2001

Laccase enzymes from Cerrena unicolor and Trametes versicolor were immobilized on the activated glass beads (CPG), silica gel (SG) and soil (SL). The heterogeneous matrices were activated by ${\gamma}$-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA), and their surfaces were coated by keratin (KER) on activated or non-activated CPG, SG and SL. The laccase activities were tested in the aqueous solution for the native and immobilized preparations using different pH and temperature conditions. By keratin coating on supports, in the cases of CPG-KER and SL-KER, the immobilization yield was increased from about 80% to 90%. Moreover, much less protein was immobilized in keratin coated matrices than in inorganic ones alone (e.g. on CPG-KER 57.6%, whereas on CPG alone 80.6%). Laccase immobilization on keratin coated inorganic matrices was generally more effective than that of non-coated matrices. Concerned to pH dependency, the optima pH for immobilized laccases generally shifted towards to higher values, 5.5-5.8 and even 5.9 in the case of keratin for C. unicolor and from 5.3 to 5.7 for T. versicolor, respectively, and decreased less gradually both in acidic and alkaline regions. The immobilized laccase was more stable against thermal denaturation. This seems particularly true at $75^{\circ}C$ in the case of C. unicolor, where the activity of immobilized enzyme is > 50% higher than that of the free enzyme. For T. versicolor the respective values were $65^{\circ}C$, and 50%.

• 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.

• Journal of Microbiology
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• v.45 no.3
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• pp.213-218
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• 2007

Trametes versicolor has a lignin degrading enzyme system, which is also involved in the degradation of diverse recalcitrant compounds. Manganese-dependent peroxidase (MnP) is one of the lignin degrading enzymes in T. versicolor. In this study, a cDNA clone of a putative MnP-coding gene was cloned and transferred into an expression vector (pBARGPE1) carrying a phosphinothricin resistance gene (bar) as a selectable marker to yield the expression vector, pBARTvMnP2. Transformants were generated through genetic transformation using pBARTvMnP2. The genomic integration of the MnP clone was confirmed by PCR with bar-specific primers. One transformant showed higher enzyme activity than the recipient strain did, and was genetically stable even after 10 consecutive transfers on non-selective medium.

• The Korean Journal of Mycology
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• v.18 no.3
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• pp.115-126
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• 1990

To establish basic techniques for protoplast fusion of Coriolus versicolor several factors affecting protoplast formation and regeneration were investigated. Protoplast isolation was at maximum with 2.5-day cultured mycelia of C. versicolor treated with the combination of two enzymes, Novozym 234 (10 mg/ml) and cellulase Onozuka R-10 (15 mg/ml), for 3-4.5 hours at $30^{\circ}C.$ As an osmotic stabilizer for stabilizing the protoplast, 0.6 M sucrose was the best for formation and regeneration of the protoplast from the mycelia of the fungus and the regeneration frequency was 3.48%. Protoplast fusion was made by a modified method of Peberdy using PEG (M.W. 4,000). The fusion frequency between two mutants of C. versicolor was 1.86% and the fusion products showed differences in growth rate and colony morphology.

• Journal of Microbiology and Biotechnology
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• v.24 no.4
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• pp.545-555
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• 2014

It has been previously demonstrated that laccases exhibit great potential for use in several industrial and environmental applications. In this paper, two laccase isoenzyme genes, lccB and lccC, were cloned and expressed in Pichia pastoris GS115. The sequence analysis indicated that the lccB and lccC genes consisted of 1,563 and 1,584 bp, and their open reading frames encoded 520 and 527 amino acids, respectively. They had 72.7% degree of identity in nucleotides and 86.7% in amino acids. The expression levels of LccB and LccC were up to 32,479 and 34,231 U/l, respectively. The recombinant laccases were purified by ultrafiltration and $(NH_4)_2SO_4$ precipitation, showing a single band on SDS-PAGE, which had a molecular mass of 58 kDa. The optimal pH and temperature for LccB were 2.0 and $55^{\circ}C$ with 2,2'-azinobis-[ 3-ethylbenzthiazolinesulfonic acid (ABTS) as a substrate, whereas LccC exhibited optimal pH and temperature at 3.0 and $60^{\circ}C$. The apparent kinetic parameters of LccB were 0.43 mM for ABTS with a $V_{max}$ value of 51.28 U/mg, and the Km and $V_{max}$ values for LccC were 0.29 mM and 62.89 U/mg. The recombinant laccases were able to decolorize five types of dyes. Acid Violet 43 (100 g/ml) was completely decolorized by LccB or LccC (2 U/ml), and the decolorization of Reactive Blue KN-R (100 g/ml) was 91.6% by LccC (2 U/ml). Thus, the study characterizes useful laccase isoenzymes from T. versicolor that have the capability of being incorporated into the treatment of similar azo and anthraquinone dyes from dyeing industries.