• 산업기술연구
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• 제21권A호
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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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• 제13권3호
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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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• 제1권1호
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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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• 제32권2호
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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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• 제5권4호
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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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• 제9권4호
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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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• 제6권6호
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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.

• 미생물학회지
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• 제36권3호
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• pp.228-235
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• 2000

지금까지의 Phanerochaete chrysosporium을 이용한 Lignin Peroxidase(LiP) 의 생산은 최적화 되지 못한 배양 조건으로 인해 매우 낮은 활성만을 얻을수 있었으며. 그 배양조건 또한 100% 산소의 주입을 요하는 일반적으로는 재현하기 어려운 조건이었다. 본 연구에서는 Phanerochaete chrysosporium PSBL-1 균줄르 이용, 다양한 배양조건의 변화를 통해 LiP의 과량생산과 그에 따른 isozyme 조성의 변화를 확인하고자 하였다. 최종적으로 $Mn^{2+}$를 제거한 배지에 질소 원인 diammonium을 48mM 로 첨가하고, 안정제로서 veratryI alcohol을 2 mM로 첨가하여, sponge에 의한 고착배양을 실시한 결과 1,800 units/l의 LiP가 생산되었다. 이러한 활성의 증가는 기존에 보고된 PSBL-1 균주의 LiP 최대 생산량인 700units/l와 비교 , 약 2.57배의 생산량 증대를 나타낸다. 생산된 LiP isozyme 분석결과 $Mn^{2+}$(2.73 mM)와 diammonium(48 mM)을 첨가하였을 경우 H1 isozyme의 과량 생산이 확인되었다. 생산된 LiP(0.4 units)를 이용하여 각각의 아조계 염료(acid yellow 9, congo red, orange II; each 50$\mu$M)에 대한 탈생능을 확인한 결과, 2분 이내에 이들 염료에 대한 탈색이 이루어지는 것을 확인할 수 있었고 분해 산물이 축적되는 것을 확인할 수 있었다.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2001년도 추계학술발표대회
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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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• 제34권4호
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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.