• Journal of Industrial Technology
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• v.21 no.A
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• pp.343-349
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• 2001

This study characterizes the growth of white rot fungi Phanerochaete chrysosporium IFO 31249) and lignin peroxidase(LiP) activity in different submerged culture media. P. chrysosporium was grown in the form of pellet of various sizes from a spore inoculum under shaking liquid culture condition. While the growth of mycelia was higher under the nitrogen-sufficient culture than under the nitrogen-limited culture, ligninase activity was relatively lower. The lignin peroxidase appeared in nitrogen-limited culture and was suppressed by excess nitrogen. High level(40U/l) of lignin peroxidase activity was obtained in the growth medium containing 1.5mM veratryl alcohol, a secondary metabolite of P. chrysosporium. Lignin peroxidase production was not observed under conditions of nitrogen sufficiency or in balanced media, suggesting that control parameters could increase the activity by manipulating the secondary metabolism.

• KSBB Journal
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• v.13 no.3
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• pp.223-230
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• 1998

Experiments for lignin peroxidase production have been conducted by aerobic fermentation of Phanerochaete chrysosporium under low shear rate and enriched oxygen environment. The result of flask cultures of white rot fungus indicated that high oxygen concentration and low shear force were essential for enhancement of lignin peroxidase production. Pentachlorophenol was readily degraded by lignin peroxidase produced in nutrient limited flask cultures. Polyurethane foam was fond to be an effective immobilization matrix of P. chrysosporium.

• Biotechnology and Bioprocess Engineering:BBE
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• v.1 no.1
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• pp.26-31
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• 1996

Since biosynthesis of lignin peroxidase from Phanerochaete chrysosporium was known to be sensitive to shear, it is interesting to understand the effects of the shear sensitivity for the overproduction of lignin peroxidase. In stirred-tank fermentor, the shear-sensitivity in lignin peroxidase biosynthesis was quantified by using Kolmogorov length scale. It was found that agitation at 80$\mu$m Kolmogorov length scale is advantageous for the production of lignin peroxidase from P. chrysosporium. To overcome the shear sensitivity in lignin peroxidase biosynthesis caused by the agitation,P. chrysosporium was immobilized on various solid carriers. The nylon-immobilized P. chrysosporium was chosen in the present study as a way to overcome the shear sensitivity at the ranges of above 50$\mu$m Kolmogorov length scale. The adhesion force between immobilized cell and carrier can be predicted by thermodynamic approach and used as a criteria to select an adequate carrier materials for immobilization.

• KSBB Journal
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• v.32 no.2
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• pp.96-102
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• 2017

The lignocellulose that is a major component of spent coffee ground was degraded and saccharified. To implement the spent coffee, after several pre-treatments, inoculation of Phanerochaete chrysosporium and solid-state fermentation were conducted. The optimal temperature of the enzymes (lignin peroxidase, manganese peroxidase, xylanase, laccase, and cellulase) for degradation of lignocellulose by P. chrysosporium was found. We also measured the maximum activity of enzymes (lignin peroxidase 0.15 IU/mL, manganese peroxidase 0.90 IU/mL, laccase 0.11 IU/mL, cellulase 5.87 IU/mL, carboxymethyl cellulase 9.52 IU/mL, xylanase 1.16 IU/mL) used for the process. As a result, 4.73 mg/mL of reduced sugar was obtained and 61.02% of lignin was degraded by solid state fermentation of P. chrysosporium on spent coffee ground.

• 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.

• 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.6 no.6
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• pp.420-424
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• 1996

Effects of exogenous veratryl alcohol addition on the growth of basidiomycete Phanerochaete chrysosporium ME-446 and the induction of lignin peroxidase activity were investigated in this study. The organism was grown in ligninolytic (low-nitrogen) culture conditions in which extracellular enzymes are produced. Analyses showed that a statistically significant decrease of cell growth was associated with the veratryl alcohol addition. The effect of veratryl alcohol addition on LiP activity was nearly instantaneous and this effect diminished with culture aging. The extent of this effect was different depending on the time of addition, which led to a speculation that there might be some other effector species which played a role in regulation of lignin peroxidase activity.

• 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.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.619-620
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• 2001

Lignin peroxidase was produced by free cells of Phanerochaete chrysosporium YU in shaking-flask batch cuture. Without aerating, the maximum activity was 785U/L. As nitrogen source, ammonium tartrate was used for LiP production and 0.02% ammonium tartrate concentration showed the highest potential for LiP prodution.

• Mycobiology
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• v.34 no.4
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• pp.159-165
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• 2006

One of the most economically viable processes for the bioconversion of many lignocellulosic waste is represented by white rot fungi. Phanerochaete chrysosporium is one of the important commercially cultivated fungi which exhibit varying abilities to utilize different lignocellulosic as growth substrate. Examination of the lignocellulolytic enzyme profiles of the two organisms Phanerochaete chrysosporium and Rhizopus stolonifer show this diversity to be reflected in qualitative variation in the major enzymatic determinants (ie cellulase, xylanase, ligninase and etc) required for substrate bioconversion. For example P. chrysosporium which is cultivated on highly lignified substrates such as wood (or) sawdust, produces two extracellular enzymes which have associated with lignin deploymerization. (Mn peroxidase and lignin peroxidase). Conversely Rhizopus stolonifer which prefers high cellulose and low lignin containg substrates produce a family of cellulolytic enzymes including at least cellobiohydrolases and ${\beta}-glucosidases$, but very low level of recognized lignin degrading enzymes.