• Korean Chemical Engineering Research
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• v.49 no.1
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• pp.101-104
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• 2011

Cellobiose dehydrogenase(CDH) as a hemoflavoenzyme is secreted out of cell in the cellulose degradation. As CDH strongly bound to amorphous cellulose, it helps cellulose hydrolysis by cellulase. CDH may have an important role of saccharification process for bioethanol production. In this study, Phanerochaete chrysosporium ATCC 32629 was selected for the production of CDH among other strains tested. The optimal temperature and pH of CDH produced by P. chrysosporium ATCC 32629 were ${55^{\circ}C}$ and 4, respectively. To improve the activity of CDH, the mutation of P. chrysosporium was performed using proton beam that has high energy level partially. As a result, P. chrysosporium mutant with the high activity was selected at 1.2 kGy in a range of 99.9% lethal rate. The CDH and $\beta$-glucosidase activities of mutant were 1.4 fold and 20 fold higher than those of wild strain. Therefore, P. chrysosporium mutant with the high activities of CDH and $\beta$-glucosidase was obtained from mutation by proton beam irradiation.

• The Korean Journal of Mycology
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• v.22 no.3
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• pp.254-259
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• 1994

The ever increasing demand for energy and the shortage of resources all over the world have generated interest in recycling renewable sources such as lignocelluloses which otherwise would go to waste and cause environmental pollution. Lignin is the incrustation material for cellulose and hemicellulose, therefore, cellulose and hemicellulose are not easily degraded. Recycling lignocellulosic wastes as agricultural material are benefit to everybody and everything. In order to improve ligninase and laccase production of Phanerochaete chrysosporium, BKM-F-1767 and Ceriporiopsis subvermispora, FP 90031-SP, were compared. The ligninase activity of P. chrysosporium was maximum on day 4.5 of shaking culture at 150 rpm 2.5 cm in a back and forth cycle. The laccase activity of C. subvermispora was maximum on day 5.5 for 2% malt extract+0.1% yeast extract+0.1% Tween 20+6 mM Benzyl alcohol culture medium at stationary state.

• Korean Journal of Microbiology
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• v.36 no.3
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• pp.228-235
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• 2000

Until now, it was diIliculi to overproduce lignin peroxidase(LiP) fiom Pl~anemchaete ch~ysosporium since the lack of optimized growth conditions. In this paper, we optimized the LIP production conditions and monitored LIP isozyines of fl chqsospoi.ium PSBL-1. The optimized condition includes sponge matrix support, no addition of $MnSO_4$, excess addition of niixogen source(48 inM diarmnonium), and addition of stabilizer(2 mM verakyl alcohol). Finally we obtained Lip activity of 1,800 unitsll. HI isozyne was overproduced when inyceliuin was cultivated in media containing $Mn^{2+}$ (2.73 inM) and excess nitrogen(48 11d4 diannnonium). Three azo dyes(acid yellow 9, congo ued, orange IT; each concenimtion of50 $\mu$M) we1-e rapidly decolorized within 2 inins by 0.4 un~t or Lip.

• Journal of the Korean Wood Science and Technology
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• v.45 no.2
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• pp.168-181
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• 2017

Whole cell of Phanerochaete chrysosporium with reducing agent was applied to verify the degradation mechanism of aromatic compounds derived from lignin precisely. Unlike the free-reducing agent experiment, various degraded products of aromatic compounds were detected under the fungal treatment. Our results suggested that demethoxylation, $C_{\alpha}$ oxidation and ring cleavage of aromatic compounds occurred under the catabolic system of P. chrysosporium. After that, degraded products stimulated the primary metabolism of fungus, so succinic acid was ultimately main degradation product of lignin derived-aromatic compounds. Especially, hydroquinone was detected as final intermediate in the degradation of aromatics and production of succinic acid. In conclusions, P. chrysosporium has an unique catabolic metabolism related to the production of succinic acid from lignin derived-aromatic compounds, which was meaningful in terms of lignin valorization.

• The Korean Journal of Mycology
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• v.21 no.4
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• pp.310-315
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• 1993

Phanerochaete chrysosporium is a white rot fungus which secrets a family of lignin-degrading enzymes under nutrient limitation. Ligninase was extracellularly produced in agitated submerged cultures of P. chrysosporium, SC 26. Addition of veratryl alcohol(4 mM), and benzyl alcohol(10 mM) with 0.1% Tween 20 to the culture medium stimulated ligninase production. However, ligninase was not detected when both treatments of veratryl alcohol and benzyl alcohol without Tween 20 were added to the medium. Addition of 0.1 % Tween 20 to the culture medium had little effect on ligninase activity. The ligninase activity was maximum on day 5-8 for veratryl alcohol, and benzyl alcohol with 0.1 % Tween 20 additive medium.

• Journal of the Korean Wood Science and Technology
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• v.34 no.3
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• pp.56-63
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• 2006

In order to evaluate the mechanism of cellulose hydrolysis, the complementary DNA encoding Glycoside Hydrolase Family (GHF)74 was cloned from Phanerochaete chrysosporium. Depending on the presence of Cellulose Binding Module (CBM), it can be classified as GHF74A or GHF74B. The GHF74A gene from P. chrysosporium (PcGHF74A) consists of 2163 bp encoding a protein of 721 amino acid residues. The PcGHF74A showed homology of 70~77% compared with the GHF74 from other filamentous fungi. The PcGHF74B, which contains CBM and is a member of family 1, was transcribed to various transcripts depending on the nature of carbon sources and their concentration. To study the possible presence of splice variants in GHF74B transcripts in P. chrysospoium, we carried out RT-PCR analysis using primers that designed based on the annotation data and sequenced data. Our result indicated that PcGHF74B was transcribed to several splicing variants in various culture conditions. Especially in the culture of 2% cellulose, three transcript products were observed. First transcript was presumed to be a full length ORF that contained 11th intron with stop codon at position 2562 bp. The second one consisted of 12 exons and 11 introns with stop codon at position 1187 bp with 7th exon. The shortest transcript consisted of 10 exons and 9 introns with stop codon at 910 bp in the 7th exon. These premature stop codon might prevent the synthesis of fully active GHF74 or contribute for the production of protein with distinct function depending on the ambient carbon sources.

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.402-405
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• 2000

Batch culture system and continuous culture system were used to investigate the removal of disperse dye using several white rot fungi. White rot fungi used in the study were Coriolus hirsutus IFO 4917, Lenzites betulina IFO 6266, Coriolus versicolor IFO 30340 and Phanerochaete chrysosporium IFO 31249. The results of the batch culture experiment showed that white rot fungi used in this study had excellent dye removal abilities. Phanerochaete chrysosporium IFO 31249 was especially effective on the removal of disperse dyes. And continuous treatment of disperse red-60 was studied under bioreactor with vertical matrix using Phanerochaete chrysosporium IFO 31249. The removal efficiency of disperse red-60 were more than 95% in 0.20 ${\sim} 1.50 $hr^{-1}$ dilution rate and 90% in $1.83h^{-1}$ dilution rate.

• Biotechnology and Bioprocess Engineering:BBE
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• v.9 no.4
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• pp.256-260
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• 2004

Melanin was decolorized by lignin peroxidase from Phanerochaete chrysosporium. This decolorization reaction showed a Michaelis-Mentens type relationship between the decolorization rate and concentration of two substrates: melanin and hydrogen peroxide. Kinetic constants of the decolorization reaction were 0.1 OD$\sub$475//min ($V_{max}$) and 99.7 mg/L ($K_{m}$) for melanin and 0.08 OD$\sub$475//min ($V_{max}$) and 504.9 ${\mu}$M ($K_{m}$) for hydrogen peroxide, respectively. Depletion of hydrogen peroxide interrupted the decolorization reaction, indicating the essential requirement of hydrogen peroxide. Pulsewise feeding of hydrogen peroxide continued the decolorizing reaction catalyzed by lignin peroxidase. These results indicate that enzymatic decolorization of melanin has applications in the development of new cosmetic whitening agents.

• Journal of Microbiology and Biotechnology
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• v.5 no.4
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• pp.218-223
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• 1995

Veratryl alcohol which has been reported as an inducer for lignin peroxidase showed different effects on the enzyme biosynthesis in Phanerochaete chrysosporium depending on the addition time. Enzyme expression was optimally induced by adding veratryl alcohol when the carbon source began to be depleted. Hydrogen peroxide, to some extent, stimulated production of lignin peroxidase, but beyond a certain concentration, inactivated lignin peroxidase. Tween 80 induced the formation of small pellets, which were resistant to the deactivation by shear stress. Lignin peroxidase production was increased twice compared with that of the control by adopting all the optimal factors in the culture system.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.30 no.3
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• pp.15-21
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• 1998

Crude enzymes of Trichoderma viride and Phanerochaete chrysosporium were evaluated for their effect to brightness and physical properties of recycled pulp from newspaper and corrugated container board. The brightness of recycled pulp from newspaper increased with crude enzymes from Trichoderma viride and Phanerochaete chrysosporium. The brightness of recycled pulp of corrugated container board increased with crude enzyme from Phanerochaete chrysosporium, but decreased with crude enzyme from Trichoderma viride. The Δbrightness with chemical bleaching of crude enzyme treated pulp was lower than that of heat killed enzyme treated pulp, but the final brightness of pulp was increased. Modification of recycled paper with crude enzymes can result in a substantial increase in physical properties with little no loss in pulp freeness.