• Korean Journal of Clinical Laboratory Science
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• v.38 no.2
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• pp.87-93
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• 2006

This study was done to know a kind and change (transition) of enzymes produceed by Streptomyces halstedii ssp. scabies SA1-27 and Streptomyces violaceusinger C1-6 which showed good lignolytic activity and a good decolorization ratio of remazol brilliant blue R(RBBR) dye. These strains were isolated from soil and identified by the author. The basal medium containg 0.2% glucose was used to measure enzyme activity, Lignin peroxidase 1 (Lip 1) was measured by the methods of Choi, and Bourbonnais and Paice. Lignin peroxidase 2 (Lip 2) was measured by the methods of Ishida et al and Ramachandra et al using 2.4-dichlorophenol(2.4 DCP), manganese peroxidase(Mnp), veratryl alcohol oxidase (VAO), and laccase. They were measured by each of the methods of Choi and Paszczynski et al, and Bourbonnais and Paice, and De Jong et al. In the results, the kind of enzymes produced by Streptomyces halstedii ssp. scabies SA1-27 were Lip 1, Lip 2, VAO, and laccase, and their activities indicated the highest value as each 4.95 nmol/mg protein, $8.45({\times}100^{-3})unit$, 10.25 nmol/mg protein, 9.20 nmol/mg protein on the sixth day of the culture and decreased gradually over time. The kind of enzymes produced by Streptomyces violaceusinger C1-6 were Lip 1, Lip 2, Mnp, VAO, and laccase, and their activities indicated the highest value as each 4.90 nmol/mg protein, $13.85({\times}100^{-3})unit$, 3.10 nmol/mg protein, 11.30 nmol/mg protein, 4.45 nmol/mg protein on the sixth day of the culture and decreased gradually over time. Consequently, the author knew the fact that there were few differences in the kind and quantity of enzymes produced by the two Streptomyces strains, but all enzyme activities indicated the highest value on the sixth day of the culture and decreased gradually over time.

• Journal of Microbiology and Biotechnology
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• v.27 no.1
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• pp.179-188
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• 2017

White-rot basidiomycetes are the organisms that decompose lignin most efficiently, and Trametes villosa is a promising species for ligninolytic enzyme production. There are several publications on T. villosa applications for lignin degradation regarding the expression and secretion of laccase and manganese peroxidase (MnP) but no reports on the identification and characterization of lignin peroxidase (LiP), a relevant enzyme for the efficient breakdown of lignin. The object of this study was to identify and partially characterize, for the first time, gDNA, mRNA, and the corresponding lignin peroxidase (TvLiP) protein from T. villosa strain CCMB561 from the Brazilian semiarid region. The presence of ligninolytic enzymes produced by this strain grown in inducer media was qualitatively and quantitatively analyzed by spectrophotometry, qPCR, and dye fading using Remazol Brilliant Blue R. The spectrophotometric analysis showed that LiP activity was higher than that of MnP. The greatest LiP expression as measured by qPCR occurred on the $7^{th}$ day, and the ABSA medium (agar, sugarcane bagasse, and ammonium sulfate) was the best that favored LiP expression. The amplification of the TvLiP gene median region covering approximately 50% of the T. versicolor LPGIV gene (87% identity); the presence of Trp199, Leu115, Asp193, Trp199, and Ala203 in the translated amplicon of the T. villosa mRNA; and the close phylogenetic relationship between TvLiP and T. versicolor LiP all indicate that the target enzyme is a lignin peroxidase. Therefore, T. villosa CCMB561 has great potential for use as a LiP, MnP, and Lac producer for industrial applications.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.3
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• pp.211-214
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• 2000

The roles of lignin peroxidase, manganese peroxidase, and laccase were inverstigated in the biodegration of pentachlorphenol (PCP) by several which rot fungi. The disappearance of pentachlorophenol from cultures of wild type strains, P. chrysosporium, Trametes sp. and of pentachlorophenol from cultures of wild type strains, P. cheysocporium, Trametes sp. and Pleurotus ap., was observed. The activities of mangnese peroxidase and laccase was detected in Trametes sp. and pleurotus sp. cultures. However, the activities showed that PCP was degraded under ligninolytic as well as nonligninoytic condicationg that lignin peroxidase, manganese peroxidase, and laccase are not essential in the biodegradation of PCP by white rot fungi.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.29 no.4
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• pp.64-72
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• 1997

백색부후균에 의한 리그닌의 분해양상을 검토하기 위해 리그닌 분해능이 우수하고 laccase활성이 높은 LKY-7 및 C. versicolor-13 균주와 manganese peroxidase 활성은 비교적 높으나 laccase활성이 전혀 나타나지 않는 LSK-27 균주로 lignosulfonate를 처리하였다. LKY-7 과 C. versicolor-13 균주에서는 lignosulfonate의 중합화 현상이 관찰되었으며 중합화는 laccase 활성 과 비례하는 것으로 나타났다. LSK-27 균주에서는 lignosulfonate의 고분자 영역이 분해되면서 탈중합화가 일어났으며 리그닌 분해 효소로는 manganese peroxidase만 검출되었다. 보조기질로 glucose를 첨가한 결과, LKY-7 균주에서는 laccase 활정이 각소하면서 중합화 현상이 어느 정도 감소하였으나 C. versicolor-13 균주는 laccase 활성의 증가와 함께 중합화도 촉진되는 것으로 나타났다. 또한 LSK-27 균주에서도 glucose 첨가에 의해 manganese peroxidase 활성이 증가되면서 lignosulfonate의 중합화가 관찰되었다. lignosulfonate 중합화에는 laccase 뿐만 아니라 manganese peroxidase도 관여하며 보조기질로서 탄소원의 종류도 영향을 미칠것으로 검토되었다.

• Journal of Microbiology and Biotechnology
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• v.10 no.6
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• pp.737-752
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• 2000

Wood-rotting basidiomycetous fungi are the most efficient degraders of lignin on earth. The white-rot fungus Phanerochaete chrysosporium has been used as a model microorganism in the study of enzymology and its application. Because of the ability of the white-rot fungus to degrade lignin, which has an irregular structure and large molecular mass, this fungus has also been studied in relation to degrading and mineralizing many environmental pollutants. The fungus includes an array of enzymes, such as lignin peroxidase (LiP), manganese-dependent peroxidase (MnP), cellobiose:quinone oxidoreductase, and $H_2O_2$-producing enzymes and also produces many other components of the ligninolytic system, such as veratryl alcohol (VA) and oxalate. In addition, the fungus has mechanisms for the reduction of degradation intermediates. The ligninolytic systems have been proved to provide reductive reactions as well as oxidative reactions, both of which are essential for the degradation of lignin and organopollutants. Further study on the white-rot fungus may provide many tools to both utilize lignin, the most abundant aromatic polymer, and bioremediate many recalcitrant organopollutants.

• Korean Journal of Environmental Agriculture
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• v.25 no.3
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• pp.211-216
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• 2006

The present research was undertaken to investigate the activities of ligninolytic enzymes and dye-decolorization capabilities of white-rotting fungi Coriolus hirsutus LD-1. The isolated white-rotting fungi (Coriolus hirsutus LD-1) produced laccase (16,388.9 U/L) and manganese-dependent peroxidase (19.81 U/L) but it did not produce lignin peroxidase. When the isolated fungi was incubated with the treatment of dyes for 8 days, the rates of decolorization of remazol brilliant blue R and bromophenol blue were 70.2% and 98%, respectively. The activity for manganese-dependent peroxidase was low, whereas that for laccase was very high. Moreover, the laccase was more effective to decolor when compared to manganese-dependent peroxidase. The results suggested that laccase of Coriolus hirsutus LD-1 might be playing an important role in the decolorization of the dyes.

• Microbiology and Biotechnology Letters
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• v.30 no.3
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• pp.287-292
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• 2002

Lignin-peroxidase (LiP) has been considered as one of the most important industrial enzymes for biodegradation of various recalcitrant toxic compounds such as chlorinated aromatic hydrocarbons and azo-dyes. Recently, several soil actinomycetes have been reported to secrete a functionally-similar lignin-peroxidase called actinomycetes lig-nin-peroxidase (ALiP). In this manuscript, we isolated over 100 morphologically distinct actinomycetes from the contaminated soils around 10 different gas stations located nearby the Kyung-An river. Among these actinomycetes screened based on the congo-red dye-decolorization activities, one newly-isolated actinomycetes named SMA-2 showed the most significant dye-decoloring activity on the congo-red plate as well as a significant ALiP activity in a yeast-extract-malt-extract liquid media supplemented with starch. The optimum SMA-2 culture condition fur ALiP production was determined and the kinetic parameters fur the SMA-2 AkIP activity were characterized. The optimally-cultured SMA-2 also exhibited the oxidation activities toward various recalcitrant aromatic compounds including phenol, 2- chlorophenol, 4- chlorophenol, 2,4- dichlorophenol ,2,6- dichlorophenol, and 2,4, f-trichlorophe - not, suggesting a potential application of SMA-2 for contaminated soil bioremediation.

• 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.

• Journal of the Korean Wood Science and Technology
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• v.28 no.4
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• pp.17-24
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• 2000

The peroxidase activity was localized cytochemically to get an insight into its precise function in lignin biosynthesis. In this work, cerium chloride ($CeCl_3$) was used as a trapping agent for hydrogen peroxide ($H_2O_2$) generated from peroxidase. Seasonal variation of peroxidase activities in cambial region of Populus, Pinus, and Ginkgo was investigated at subcellular levels. Under transmission electron microscopy, electron dense deposits of cerium perhydroxide formed by reaction with $H_2O_2$ were observed in cambium and its immediate derivatives. The staining with $CeCl_3$ in cambium varied with growth seasons. The strongest $H_2O_2$ accumulation, regardless of tree species, appeared in May. Staining pattern of $CeCl_3$ in the cambium of poplar indicated that the production of peroxidase started in March before the opening of buds and reached the highest in May and then declined in August. Ginkgo and Pinus showed relatively late generation of $H_2O_2$ production when compared with Populus. Although Ginkgo and Pinus are classified into gymnosperms, however, the generation of peroxidase production and its duration was different from each other. Little staining appeared in all the tree samples collected in September before falling the leaves.

• 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.