Identification, Ligninolytic Enzyme Activity and Decolorization Potential of Two Fungi Isolated from a Distillery Effluent Contaminated Site

2007 ◽  
Vol 183 (1-4) ◽  
pp. 165-176 ◽  
Author(s):  
Deepak Pant ◽  
Alok Adholeya
Keyword(s):  
Enzyme Activity ◽  
Ligninolytic Enzyme ◽  
Contaminated Site ◽  
Distillery Effluent

scholarly journals Trametes suaveolens as ligninolytic enzyme producer

2013 ◽  
pp. 437-444 ◽  
Author(s):  
Aleksandar Knezevic ◽  
Ivan Milovanovic ◽  
Mirjana Stajic ◽  
Jelena Vukojevic
Keyword(s):  
Enzyme Activity ◽  
Solid State ◽  
Wheat Straw ◽  
Solid State Fermentation ◽  
Nitrogen Concentration ◽  
Pollution Prevention ◽  
Ligninolytic Enzyme ◽  
Species Selection ◽  
Submerged Cultivation ◽  
Phenol Red

Species of the genus Trametes represent one of the most efficient lignin-degraders which can be attributed to a well developed ligninolytic enzyme system. Current trends are screening of ability of new species to produce these enzymes, as well as the optimization of conditions for their overproduction. Therefore, the aim of the study was to evaluate the potential of T. suaveolens to synthesize laccase and Mn-oxidizing peroxidases during fermentation of the selected plant raw materials. Level of enzyme activities was measured on 7, 10 and 14th day of submersion, as well as the solid-state fermentation of wheat straw and oak sawdust in the presence of NH4NO3 in previously determined optimal nitrogen concentration of 25 mM. The enzyme activity was determined spectrophotometrically using ABTS and phenol red as the substrates. The highest level of laccase activity (1087.1 U/L) was noted after 7 days of wheat straw solid-state fermentation, while during the submerged cultivation the production of the enzyme was not noted. Submerged cultivation in oak sawdust-enriched medium was the optimal for activity of Mn-dependent peroxidase (1767.7 U/L on day 14) and Mn-independent peroxidase (1113.7 U/L on day 7). Introduction of T. suaveolens to produce ligninolytic enzyme represented the base for further study, as well as the determination of relation between enzyme activity and rate of lignin degradation. It could lead to greater possibility of fungal species selection with high delignification capacity, which could take participation in sustainable production of food, feed, fibres, and energy, environmentally friendly pollution prevention, and bioremediation.

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]

scholarly journals Regulation of Respiratory and Ligninolytic Enzyme Activity of <i>Lentinula edodes</i> by Selenium

2013 ◽  
Vol 03 (08) ◽  
pp. 31-36 ◽  
Author(s):  
Regiane Gonçalves Feitosa Leal Nunes ◽  
Jose Maria Rodrigues da Luz ◽  
Elizabete Fantuzzi ◽  
Maria Catarina Megumi Kasuya ◽  
Maria Cristina Dantas Vanetti
Keyword(s):  
Enzyme Activity ◽  
Lentinula Edodes ◽  
Ligninolytic Enzyme

Survey of ectomycorrhizal, litter-degrading, and wood-degrading Basidiomycetes for dye decolorization and ligninolytic enzyme activity

2010 ◽  
Vol 98 (4) ◽  
pp. 483-504 ◽  
Author(s):  
Leonardo Casieri ◽  
Antonella Anastasi ◽  
Valeria Prigione ◽  
Giovanna Cristina Varese
Keyword(s):  
Enzyme Activity ◽  
Dye Decolorization ◽  
Ligninolytic Enzyme

scholarly journals The mycelial growth and ligninolytic enzyme activity of cauliflower mushroom (Sparassis latifolia)

2017 ◽  
Vol 13 (4) ◽  
pp. 158-163
Author(s):  
Hong-Duck Sou ◽  
Rhim Ryoo ◽  
Kang-Hyeon Ka ◽  
Hyun Park
Keyword(s):  
Enzyme Activity ◽  
Mycelial Growth ◽  
Ligninolytic Enzyme

scholarly journals Production, purification, and kinetics of the poly-β-hydroxybutyrate depolymerase from Microbacterium paraoxydans RZS6: A novel biopolymer-degrading organism isolated from a dumping yard

2019 ◽  
Author(s):  
RZ Sayyed ◽  
SJ Wani ◽  
Abdullah A. Alyousef ◽  
Abdulaziz Alqasim ◽  
Asad Syed
Keyword(s):  
Enzyme Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Scale Up ◽  
Sodium Dodecyl ◽  
Contaminated Site ◽  
Rrna Gene ◽  
Minimal Salt Medium ◽  
Phb Depolymerase ◽  
Microbacterium Paraoxydans ◽  
Extracellular Phb Depolymerase

AbstractPoly-β-hydroxybutyrate (PHB) depolymerase can decompose biodegradable polymers and therefore has great commercial significance in the bioplastic sector. However, few reports have described PHB depolymerases based on isolates obtained from plastic-contaminated sites that reflect the potential of the source organism. In this study, we evaluated Microbacterium paraoxydans RZS6 as a producer of extracellular PHB depolymerase isolated from a plastic-contaminated site in the municipal area of Shahada, Maharashtra, India, for the first time. The isolate was identified using the polyphasic approach, i.e., 16S rRNA gene sequencing, gas chromatographic analysis of fatty acid methyl esters, and BIOLOG identification, and was found to hydrolyze PHB on minimal salt medium containing PHB as the only source of carbon. Both isolates produced PHB depolymerase at 30°C within 2 days and at 45°C within 4 days. The enzyme was purified most efficiently using an octyl-sepharose CL-4B column, with the highest purification yield of 6.675 U/mg/mL. The enzyme required Ce2+ and Mg2+ ions but was inhibited by Fe2+ ions and mercaptoethanol. Moreover, enzyme kinetic analysis revealed that the enzyme was a metalloenzyme requiring Mg2+ ions, with optimum enzyme activity at 45°C (thermophilic) and under neutrophilic conditions (optimum pH = 7). The presence of Fe2+ ions (1 mM) and mercaptoethanol (1000 ppm) completely inhibited the enzyme activity. The molecular weight of the enzyme (40 kDa), as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, closely resembled that of PHB depolymerase from Aureobacterium saperdae. Scale-up from the shake-flask level to a laboratory-scale bioreactor further enhanced the enzyme yield. Our findings highlighted the applicability of M. paraoxydans as a producer of extracellular PHB depolymerase isolated from a plastic-contaminated site in the municipal area of Shahada, Maharashtra, India.

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