• 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.

• Korean Journal of Microbiology
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• v.39 no.3
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• pp.201-205
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• 2003

Laccase, lignin- and manganese peroxidase are implicated in the lignin degradation. The nucleotide sequences of four copper-binding domains in fungal laccases, and heme-binding domains of lignin- and manganese peroxidases are well conserved, and therefore these short fragments can be used for the PCR for the gene amplification. We synthesized several PCR primers according to their sequences, and run PCR to amplifiy the lignin degrading genes of Trametes versicolor isolated in Korea. PCR products were cloned with pGEM-T vector in order to determine their nucleotide sequences. A laccase fragment (1.3 kb) showed 65-97％ homologies, lignin peroxidase fragment (185 bp) showed 80-95％ homologies, and manganese peroxidase fragment (443 bp) showed 61-83％ homologies when compared with other white-rot fungal enzymes.

• 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.

• Clean Technology
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• v.23 no.4
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• pp.408-412
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• 2017

Pigment red 53:1 is a dye used in various products as a component of the inks, suspected of being carcinogenic. Thus, the environmental and occupational issues related to it are important. The enzyme-based approach with reusability has advantages to consume less energy and generate less harsh side- products compared to the conventional strategies including separations, microbe, and electrochemical treatment. The degradation of Pigment red 53:1 by the lignin peroxidase immobilized on the surface of magnetic particles has been studied. The immobilization of the peroxidase was conducted on magnetic particle surface with the treatment of polyethyleneimine, glutaraldehyde, and the peroxidase, in sequence. The immobilization was confirmed using X-ray photon spectroscopy. The absorbance peak of the pigment was monitored at 495 nm of UV/Vis spectrum with respect to time to calculate the catalytic activities of the pigment for the immobilized lignin peroxidase. For the comparison, the absorbance of the lignin peroxidase free in solution was also monitored. The catalytic rate constant values for the free lignin peroxidases and the immobilized those were 0.51 and $0.34min^{-1}$, respectively. The reusable activity for the immobilized lignin peroxidase was kept to 92% after 10 cycles. The stabilities for heat and storage were also investigated for both cases.

• KSBB Journal
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• v.17 no.1
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• pp.14-19
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• 2002

The objective of this study is to investigate optimum condition for lignin peroxidase production by white rot fungi Phanerochaete chysosporium IFO 31249 immobilized in a rotating bioreactor. The maximum lignin peroxidase activity of batch culture in rotating bioreactor was 300 U/L. The optimum rotating speed and packing ratio of support for lignin peroxidase production in a rotating bioreactor were 1 rpm and 20%, respectively. The optimum concentration of $MnSO_4$$\cdot$$H_2O$ for manganese-dependent peroxidase production in a rotating bioreactor was 50 ppm. The sufficient supply of oxygen was the most important factor to achieve maximum lignin peroxidase production. It was possible to produce lignin peroxidase (LiP) and manganese-dependent peroxidase (MnP) for at least 3 times successive repeated-batch cultures, respectively.

• KSBB Journal
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• v.15 no.1
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• pp.22-26
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• 2000

Kraft Lignin which is produced abundantly in pulp industry, was chemically degraded into small oligomers and polymerized using horseradish peroxidase. Lignin acidolysis was optimized by controlling reaction time and HCI concentration. Acidolyzed lignin was polymerized and copolymers of acidolyzed lignin and phenol or p-cresol were synthesized. 70% of kraft lignin was degraded after acidolysis. Number average molecular weight of all lignin polymers were from 8,500 to 14,000 and did not show large difference. Differential scanning calorimeter analysis showed that acidolyzed lignin did not show any melting temparature under $300^{\circ}C$, which indicates that newly synthesized lignin polymers can be used in industry under mild condition.

• 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.

• 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.

• 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.

• Biotechnology and Bioprocess Engineering:BBE
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• v.8 no.2
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• pp.130-134
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• 2003

A visual method for the selective screen Eng of lignin degrading enzymes, produced by white rot fungi (WRF), was investigated by the addition of coloring additives to solid media. Of the additives used in the enzyme production media, guaiacol and RBBR could be used for the detection of lignin peroxidase (LiP), manganese peroxidase (MnP) and lactase. Syringaldazine and Acid Red 264 were able for the detection of both the MnP and lactase, and the LiP and laccase, respectively, and a combination of these two additives was able to detect each of the ligninases produced by the WRF on solid media.