scholarly journals The Influence of Inducers on the Coltricia cinnamomea Laccase Activity and its Ability to Degrade POME

2021 ◽  
Vol 13 (2) ◽  
pp. 243-249
Author(s):  
Yohanes Bernard Subowo ◽  
Arwan Sugiharto
Keyword(s):  
Palm Oil ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Laccase Activity ◽  
Ligninolytic Enzymes ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Growth Media ◽  
Palm Oil Mill ◽  
Low Activity

Some species of Basidiomycetes, specifically white rot groups, produce three ligninolytic enzymes, namely, Lignin Peroxidase (LiP), Manganese Peroxidase (MnP) and Laccase (Lac), which have low activity in degrading Palm Oil Mill Effluent (POME). The research objective was to obtain the data on the ability of the Coltricia cinnamomea to produce LiP, MnP, and Lac enzymes to degrade POME. This research also studied the effect of sucrose, alcohol, veratryl alcohol, CuSO4 and ZnSO4,as inducers. Isolates of Coltricia cinnamomea, which were stored in a PDA media at -20℃ were obtained from the Microbiology section of the Research Center for Biology (LIPI). Furthermore, the growth media used were DM, Bean sprout Extract (TE) and PDB. The result indicated that PDB is the most suitable growth media for the production of ligninolytic enzymes, because in this medium these enzymes showed the highest activity. It was also observed that sucrose increased the laccase activity by 40.80%. Furthermore, Coltricia cinnamomea was able to reduce the concentration of Poly R-478 by 60.74%, after the addition of ZnSO4. In addition, it degraded and decreased the color and COD of POME, by 72.63% and 91.19% respectively, after the addition of veratryl alcohol, and incubation for 10 days. Therefore, this fungus can be used to degrade POME in order to prevent environmental pollution. Coltricia cinnamomea has not been used for POME degradation. By using Coltricia cinnamomea, we  obtained new data regarding the activity of laccase and its ability to degrade POME. 

scholarly journals Lignin-degrading activity and ligninolytic enzymes of different white-rot fungi: effects of manganese and malonate

1997 ◽  
Vol 75 (1) ◽  
pp. 61-71 ◽  
Author(s):  
Tamara Vares ◽  
Annele Hatakka
Keyword(s):  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
White Rot Fungi ◽  
Ligninolytic Enzymes ◽  
Growth Conditions ◽  
Fungal Species ◽  
White Rot ◽  
Trametes Hirsuta ◽  
Air Atmosphere ◽  
Trametes Trogii

Ten species of white-rot fungi, mainly belonging to the family Polyporaceae (Basidiomycotina), were studied in terms of their ability to degrade14C-ring labelled synthetic lignin and secrete ligninolytic enzymes in liquid cultures under varying growth conditions. Lignin mineralization by the fungi in an air atmosphere did not exceed 14% within 29 days. Different responses to the elevated Mn2+concentration and the addition of a manganese chelator (sodium malonate) were observed among various fungal species. This could be related with the utilization of either lignin peroxidase (LiP) or manganese peroxidase (MnP) for lignin depolymerization, i.e., some fungi apparently had an LiP-dominating ligninolytic system and others an MnP-dominating ligninolytic system. The LiP isoforms were purified from Trametes gibbosa and Trametes trogii. Isoelectric focusing of purified ligninolytic enzymes revealed the expression of numerous MnP isoforms in Trametes gibbosa, Trametes hirsuta, Trametes trogii, and Abortiporus biennis grown under a high (50-fold) Mn2+level (120 μM) with the addition of the chelator. In addition, two to three laccase isoforms were detected. Key words: white-rot fungi, lignin degradation, lignin peroxidase, manganese peroxidase, manganese, malonate.

High production of ligninolytic enzymes from white rot fungi in cereal bran liquid medium

1999 ◽  
Vol 45 (7) ◽  
pp. 627-631 ◽  
Author(s):  
M A Pickard ◽  
H Vandertol ◽  
R Roman ◽  
R Vazquez-Duhalt
Keyword(s):  
Manganese Peroxidase ◽  
White Rot Fungi ◽  
Alcohol Oxidase ◽  
Ligninolytic Enzymes ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Laccase Production ◽  
Good Growth ◽  
Malt Extract ◽  
Cereal Bran

White rot fungi from the University of Alberta Mold Herbarium, identified as able to degrade aromatics from a study of PCB metabolism, were examined for production of ligninolytic enzymes. Production of lignin peroxidase, manganese peroxidase, laccase, and veratryl alcohol oxidase were monitored during growth in different media. Good growth but low enzyme production occurred in a glucose - malt extract - yeast extract medium. Media containing 2% cereal bran in 60 mM phosphate buffer supported high levels of laccase production, up to 13 000 U/L in Coriolopsis gallica UAMH 8260 and manganese peroxidase activity up to 1100 U/L in Bjerkandera adusta UAMH 8258. Cereal bran media supported higher laccase production than 2,5-xylidine and higher manganese peroxidase production than a medium containing manganous ion plus veratryl alcohol.Key words: cereal bran, laccase, manganese peroxidase, white rot fungi.

scholarly journals Enhanced Production of Ligninolytic Enzymes by a Mushroom Stereum ostrea

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
K. Y. Usha ◽  
K. Praveen ◽  
B. Rajasekhar Reddy
Keyword(s):  
Solid State ◽  
Copper Sulphate ◽  
White Rot Fungi ◽  
Ligninolytic Enzymes ◽  
Tween 80 ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Tween 20 ◽  
Laccase Production ◽  
Enhanced Production

The white rot fungi Stereum ostrea displayed a wide diversity in their response to supplemented inducers, surfactants, and copper sulphate in solid state fermentation. Among the inducers tested, 0.02% veratryl alcohol increased the ligninolytic enzyme production to a significant extent. The addition of copper sulphate at 300 μM concentration has a positive effect on laccase production increasing its activity by 2 times compared to control. Among the surfactants, Tween 20, Tween 80, and Triton X 100, tested in the studies, Tween 80 stimulated the production of ligninolytic enzymes. Biosorption of dyes was carried out by using two lignocellulosic wastes, rice bran and wheat bran, in 50 ppm of remazol brilliant blue and remazol brilliant violet 5R dyes. These dye adsorbed lignocelluloses were then utilized for the production of ligninolytic enzymes in solid state mode. The two dye adsorbed lignocelluloses enhanced the production of laccase and manganese peroxidase but not lignin peroxidase.

scholarly journals Lignolytic Enzymes Production from Selected Mushrooms

2015 ◽  
Vol 3 (2) ◽  
pp. 308-313 ◽  
Author(s):  
H.M. Shantaveera Swamy ◽  
Ramalingappa
Keyword(s):  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Western Ghats ◽  
Agar Plate ◽  
Ligninolytic Enzymes ◽  
Enzyme Assays ◽  
Lignolytic Enzymes ◽  
Plate Assay

In this paper, ligninase enzymes produced by selected mushrooms have been reported. We collected mushrooms from Western Ghats, most of them were edible food. Thirty samples isolated were tested using a plate assay through direct agar plate assay by using ABTS, decolourisation containing the fifteen isolates were able to decolourise the dye, indicating a lignin-degrading ability. Spectrophotometric enzyme assays from all selected isolates were carried out to examine the production of Ligninolytic enzymes (Laccase, lignin peroxidase and manganese peroxidase). Ten selected isolates produced all three kinds of enzymes tested. Lignolytic enzymes are groups of enzymes these are actively involved in bioremediation.Int J Appl Sci Biotechnol, Vol 3(2): 308-313 DOI: http://dx.doi.org/10.3126/ijasbt.v3i2.12732 

Enhanced Production of Ligninolytic Enzymes by Ganoderma lucidum IBL-06 Using Lignocellulosic Agricultural Wastes

2010 ◽  
Vol 8 (1) ◽  
Author(s):  
Muhammad Asgher ◽  
Yasir Sharif ◽  
H.N. Bhatti
Keyword(s):  
Rice Straw ◽  
Lignin Peroxidase ◽  
Ganoderma Lucidum ◽  
Ligninolytic Enzymes ◽  
Tween 80 ◽  
Veratryl Alcohol ◽  
Inoculum Size ◽  
Enhanced Production ◽  
Lignocellulosic Substrates ◽  
Ssf Process

An indigenous novel strain of Ganoderma lucidum IBL-06 was investigated for the production of ligninolytic enzymes including lignin peroxidase (LiP), manganese peroxidase (MnP) and laccase using different lignocellulosic substrates in still culture solid-state fermentation (SSF). The fermentation flasks were inoculated and incubated at 35°C for 14 days. Samples were harvested after every 48 h to study the profile of ligninolytic enzymes produced by the fungus on different substrates. Maximum enzyme activities were noted on 10th day of incubation on rice straw. Ganoderma lucidum IBL-06 produced highest activities of lignin peroxidase (LiP) among the lignolytic enzymes. By optimizing the SSF process, maximum activities of LiP (2185 IU/ml), MnP (1972 IU/ml) and laccase (338 IU/ml) were achieved after three days incubation of rice straw at pH 4.5; temperature, 35°C; moisture, 75% and inoculum size, 6 ml, using fructose as carbon source, urea as nitrogen source, Tween-80 as surfactant and veratryl alcohol as mediator.

scholarly journals Quantitative Evaluation of the Production of Ligninolytic Enzymes- Lignin Peroxidase and Manganese Peroxidase by P. Sajor Caju During Coir Pith Composting

CORD ◽  
2012 ◽  
Vol 28 (1) ◽  
pp. 10 ◽  
Author(s):  
Radhakrishnan S
Keyword(s):  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Tamil Nadu ◽  
Lignin Content ◽  
Ligninolytic Enzymes ◽  
Oxidative Enzymes ◽  
Aquatic Life ◽  
Coir Pith ◽  
Coir Fibre ◽  
Pleurotus Sajor Caju

Coir is the natural hard fruit fibre extracted from the exocarp of the coconut. The fibre has over 40 percent lignin and is spun into yarn and rope. Coir is used globally for manufacturing floor coverings as home furnishing. The Coir Industry enjoys the status as the largest cottage industry in Kerala giving employment to over a million people, of which 80 percent constitute women. Coir pith is a biomass residue generated during the extraction of coir fibre from coconut husk. Coir pith produced during coir fibre extraction is of environmental concern as its dumping on shore line and leaching of its constituents alter water quality and aquatic life. Management of coir pith is a major problem with all coir industrialists. Hillocks of coir pith accumulate in the vicinities of coir fibre extraction units in Kerala, Tamil Nadu, Andhra Pradesh, Karnataka, and Orissa. These agricultural wastes have traditionally been disposed by burning which resulted in various environmental problems. Therefore, composting is an alternate way to dispose coir pith and is of critical importance. Ligninolytic enzyme production during coir pith composting by Pleurotus sajor caju has been studied in detail. Pleurotus sajor caju produces oxidative enzymes which degrade lignin in the presence of urea as nitrogen source. Substitution of urea with vegetative sources has resulted in the vigorous growth of the mushroom which leads to decreased lignin content and C: N ratio in the biodegraded coir pith. Combination of Azolla and Soya hulls as biological supplements was observed to be the best substitute for lignin peroxidase and manganese peroxidase production. Activity of manganese peroxidase and lignin peroxidase was maximum on the twentieth day of fermentation of coir pith. The level of enzyme activity during biological composting using vegetative sources was compared with the conventional process using urea. The enzyme profile exhibited variation with change in substrate and duration of decomposition. The colonization of Pleurotus sajor caju by its utilization leads to biochemical changes in coir pith converting it into an ideal plant nutrient.

scholarly journals Aktivitas enzim ligninolitik Pleurotus ostreatus pada media yang mengandung TKKS dan aplikasinya untuk dekolorisasi zat warna (Activity of ligninolytic enzyme of Pleurotus ostreatus on media containing OPEFB and their application for dyes decolorization)

2019 ◽  
Vol 87 (1) ◽  
Author(s):  
Firda DIMAWARNITA ◽  
TRI - PANJI
Keyword(s):  
Enzyme Activity ◽  
Lignin Peroxidase ◽  
Congo Red ◽  
Pleurotus Ostreatus ◽  
Ligninolytic Enzymes ◽  
Ligninolytic Enzyme ◽  
White Rot ◽  
Enzyme Extract ◽  
Media Composition ◽  
Dyes Decolorization

Ligninolytic enzymes are known as extracellular enzymes produced by the white rot fungi class of basidiomycetes. One of the most well-known fungi of the white rot fungus isPleurotus ostreatus. The aim of this study to calculate the activity of ligninolytic enzymes in the growth media of Pleurotus ostreatusand their application in decolorization of dye colour. The ligninolytic enzyme extract obtained was used to decolorize bluedyes (MethyleneBlue)and red dyes(Congo Red). The highest laccase enzyme activity was in the first month of 0.35 U/mL with E1 media composition; the highest manganese peroxidase (MnP) enzyme activity was in the fourth month at 31.818 U / mL with E4 media composition; and the highest lignin peroxidase (LiP) enzyme activity was in the fifth month at 0.269 U / mL with E1 media composition. The enzyme extract obtained was then applied to decolorize red and blue dyes. Decolorization of dyes was measured using spectrophotometry with a blue wavelength of 470 nm and red 685 nm. The highest reduction in decolorization of blue dye and red dye was 12 hours with concentration of enzyme addition of 0.5%. Based on these results, ligninolytic enzymes potentiallyto be developed as bioactive agents for detergents.[Keywords: decolorization, laccase, mangan peroxidase, lignin peroxidase, spectrofotometry] AbstrakEnzim ligninolitik dikenal sebagai enzim ekstraseluler yang dihasilkan oleh jamur pelapuk putih golongan basidiomycetes. Salah satu jamur dari golongan jamur pelapuk putih yang banyak dikenal adalah Pleurotus ostreatus. Penelitian ini bertujuan menghitung aktivitas enzim ligninolitik pada media pertumbuhan jamur tiram  (Pleurotus ostreatus) dan aplikasinya dalam dekolorisasi zat warna.  Ekstrak enzim ligninolitik yang didapatkan kemudian dimanfaatkan untuk dekolorisasi zat warna biru(Methylene Blue)dan merah (Congo Red). Aktivitas enzim lakase tertinggi ada pada bulan pertama sebesar 0,35 U/mL dengan komposisi media E1; aktivitas enzim mangan peroksidase (MnP) tertinggi ada pada bulan keempat sebesar 31,818 U/mL dengan komposisi media E4; dan aktivitas enzim lignin peroksidase (LiP) tertinggi ada pada bulan kelima sebesar 0,269 U/mL dengan komposisi media E1. Ekstrak enzim yang didapat kemudian diaplikasikan untuk dekolorisasi zat warna merah dan biru. Dekolorisasi zat warna diukur menggunakan spektrofotometri dengan panjang gelombang biru pada 470 nm dan merah pada 685 nm. Penurunan dekolorisasi zat warna birudan zat warna merahtertinggi selama 12jam dengan konsentraasi penambahan enzim sebesar 0,5%.Berdasarkan hasil tersebut, enzim ligninolitik sangat potensial untuk dikembangkan sebagai agen bioaktif untuk deterjen.[Kata kunci: dekolorisasi, lakase, mangan peroksidase, lignin peroksidase,  spektrofotometri]

A new versatile peroxidase from Pleurotus

2001 ◽  
Vol 29 (2) ◽  
pp. 116-122 ◽  
Author(s):  
F. J. Ruiz-Dueñas ◽  
S. Camarero ◽  
M. Pérez-Boada ◽  
M. J. Martínez ◽  
A. T. Martínez
Keyword(s):  
Electron Transfer ◽  
Chemical Modification ◽  
Binding Site ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Veratryl Alcohol ◽  
Substrate Oxidation ◽  
Molecular Models ◽  
Electron Transfer Pathway ◽  
High Affinity

Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanero-chaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn2+, hydro-quinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn2+-binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn2+-binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed.

scholarly journals Influence of cellobiose oxidase on peroxidases from Phanerochaete chrysosporium

1993 ◽  
Vol 293 (2) ◽  
pp. 431-435 ◽  
Author(s):  
P Ander ◽  
G Sena-Martins ◽  
J C Duarte
Keyword(s):  
Cytochrome C ◽  
Horseradish Peroxidase ◽  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Veratryl Alcohol ◽  
Lag Phase ◽  
And Function ◽  
Compound Ii ◽  
Catalytic Cycles

Reduction of H2O2-oxidized manganese peroxidase (MnP), lignin peroxidase and, to some extent, horseradish peroxidase, was studied in the presence of cellobiose oxidase (CbO) and cellobiose. It was found that the reversion rates for MnP compound II and lignin peroxidase compound II back to native enzymes increased significantly in the presence of CbO and cellobiose. However, the reduction of cytochrome c by CbO plus cellobiose was 40 times faster than the reduction of MnP compound II. Also, the lag phase before reversion to the native states decreased for all three peroxidases in the presence of CbO and cellobiose. Active CbO did not repress formation of compounds I or II of the peroxidases, and Mn2+/veratryl alcohol reduced compound II of the peroxidases much more rapidly than did active CbO. This indicates that, in the presence of Mn2+ or veratryl alcohol, MnP and lignin peroxidase can complete their catalytic cycles and function normally without interference from CbO. Without the presence of peroxidase substrates, active CbO reduced compound II of the above peroxidases.

Comparative production of ligninolytic enzymes by Phanerochaete chrysosporium and Polyporus sanguineus

2009 ◽  
Vol 55 (12) ◽  
pp. 1397-1402 ◽  
Author(s):  
Paramjit Kaur Bajwa ◽  
Daljit Singh Arora
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Ligninolytic Enzymes ◽  
Culture Conditions ◽  
Malt Extract ◽  
Mineral Salts ◽  
Wide Range ◽  
Extract Medium ◽  
Malt Extract Medium

The aim of the present study was to compare the effect of a wide range of culture conditions on production of ligninolytic enzymes by Polyporus sanguineus and Phanerochaete chrysosporium . Lignin peroxidase production by P. sanguineus was comparable with that of P. chrysosporium, although the culture conditions giving the highest yield varied greatly between the two fungi. Highest yield of manganese peroxidase by P. sanguineus obtained in 0.5% malt extract medium and peptone or malt extract supplemented mineral salts broth could not be surpassed by P. chrysosporium in any of the optimization experiments. In addition to lignin peroxidase and manganese peroxidase, P. sanguineus also produced laccase, which was best expressed in malt extract medium supplemented with sugarcane bagasse.

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