Azo Dyes Decolourisation by ABTS-oxidases (Laccases) from a Fungus from Tropical Tree (original) (raw)
Related papers
Applied Microbiology and Biotechnology, 2010
The jelly fungus Auricularia auricula-judae produced an enzyme with manganese-independent peroxidase activity during growth on beech wood (∼300 U l −1 ). The same enzymatic activity was detected and produced at larger scale in agitated cultures comprising of liquid, plant-based media (e.g. tomato juice suspensions) at levels up to 8,000 U l −1 . Two pure peroxidase forms (A. auricula-judae peroxidase (AjP I and AjP II) could be obtained from respective culture liquids by three chromatographic steps. Spectroscopic and electrophoretic analyses of the purified proteins revealed their heme and peroxidase nature. The N-terminal amino acid sequence of AjP matched well with sequences of fungal enzymes known as "dye-decolorizing peroxidases". Homology was found to the N-termini of peroxidases from Marasmius scorodonius (up to 86%), Thanatephorus cucumeris (60%), and Termitomyces albuminosus (60%). Both enzyme forms catalyzed not only the conversion of typical peroxidase substrates such as 2,6-dimethoxyphenol and 2,2′-azino-bis(3-ethylthiazoline-6sulfonate) but also the decolorization of the high-redox potential dyes Reactive Blue 5 and Reactive Black 5, whereas manganese(II) ions (Mn 2+ ) were not oxidized. Most remarkable, however, is the finding that both AjPs oxidized nonphenolic lignin model compounds (veratryl alcohol; adlerol, a nonphenolic β-O-4 lignin model dimer) at low pH (maximum activity at pH 1.4), which indicates a certain ligninolytic activity of dye-decolorizing peroxidases.
BioResources
Lignin peroxidase (LiP), which has been studied extensively in white-rot basidiomycetes and their potential to degrade dyes from textile wastewater, plays a role in the biodegradation of lignin from pulp and paper industry wastewater, as well as agricultural waste. Lignin peroxidase (LsLiP) was successfully purified from the newly isolated Lentinus squarrosulus MPN12 with a 47.1-fold purification and a 15.7% yield. After 48 h-incubation, LsLiP was able to decolorize all tested dyes up to 92% for Acid Blue 62 (NY3), followed by Porocion Brilliant blue HGR (PB, 73.5%), Acid Blue 281 (NY5, 70.5%), Acid Blue 113 (IN13, 61%), Acid red 266 (NY7, 56%), and 34.5% for Acid red 299 (NY1), compared to the negative control with the heat-denatured enzyme. The biodegradation potential of LsLiP was further suggested by the change of lignin structure based on Fourier transform infrared (FTIR) analyses. Lignin structure was noticeably changed before and after LsLiP treatment, especially in the finge...
Applied Microbiology and Biotechnology, 2013
Catalytic and physicochemical properties of representative fungal dye-decolorizing peroxidases (DyPs) of wood-(WRF) and litter-decomposing white-rot fungi (LDF) are summarized and compared, including one recombinant Mycetinis scorodonius DyP (rMscDyP; LDF), the wild-type Auricularia auricula-judae DyP (AauDyP; WRF), and two new DyPs secreted by the jelly fungi Exidia glandulosa (EglDyP; WRF) and Mycena epipterygia (MepDyP; LDF). Homogeneous preparations of these DyPs were obtained after different steps of fast protein liquid chromatography, and they increase the total number of characterized fungal DyP proteins to eight. The peptide sequences of AauDyP, MepDyP, and EglDyP showed highest homologies (52-56 %) to the DyPs of M. scorodonius. Five out of the eight characterized fungal DyPs were used to evaluate their catalytic properties compared to classic fungal and plant heme peroxidases, namely lignin peroxidase of Phanerochaete chrysosporium (PchLiP; WRF), versatile peroxidase of Bjerkandera adusta (BadVP; WRF), and generic peroxidases of Coprinopsis cinerea (CiP) and Glycine max (soybean peroxidase0SBP). All DyPs tested possess unique properties regarding the stability at low pH values: 50-90 % enzymatic activity remained after 4-h exposition at pH2.5, and the oxidation of nonphenolic aromatic substrates (lignin model compounds) was optimal below pH3. Furthermore, all DyPs efficiently oxidized recalcitrant dyes (e.g., Azure B) as well as the phenolic substrate 2,6-dimethoxyphenol. Thus, DyPs combine features of different peroxidases on the functional level and may be part of the biocatalytic system secreted by fungi for the oxidation of lignin and/or toxic aromatic compounds.
Biochemical features of dye‐decolorizing peroxidases: Current impact on lignin degradation
Biotechnology and Applied Biochemistry, 2020
Dye‐decolorizing peroxidases (DyP) were originally discovered in fungi for their ability to decolorize several different industrial dyes. DyPs catalyze the oxidation of a variety of substrates such as phenolic and nonphenolic aromatic compounds. Catalysis occurs in the active site or on the surface of the enzyme depending on the size of the substrate and on the existence of radical transfer pathways available in the enzyme. DyPs show the typical features of heme‐containing enzymes with a Soret peak at 404–408 nm. They bind hydrogen peroxide that leads to the formation of the so‐called Compound I, the key intermediate for catalysis. This then decays into Compound II yielding back Fe(III) at its resting state. Each catalytic cycle uses two electrons from suitable electron donors and generates two product molecules.DyPs are classified as a separate class of peroxidases. As all peroxidases they encompass a conserved histidine that acts as the fifth heme ligand, however all primary DyP s...
Mycoremediation: Decolourization Potential of Fungal Ligninolytic Enzymes
Book Chapter, 2017
Textile industry is the most avid user for dyes. Rapidly growing interest in developing more synthetic commercial dyes from its native to endeavour human needs contributed to aesthetic problems to the environment and public health. Increasing concerns about colours in the effluents lead to worldwide efforts to develop more effective colour removal processes. However, the physical and chemical treatment methods of the discharge effluents are not economically feasible even if some of them are inefficient nowadays. Furthermore, liberating the hazardous product from secondary pollution from these methods acquires valid waste management system. Without proper discharge, azo dyes and associated chemicals may induce mutagenesis leading to toxicity in aquatic plants and animals. Utilization of mycoremediation of dyes as green chemistry technology has yet become a promising approach due to its clear picture of cost, eco-friendly and environmentally benign process as an alternative green solution to replace or supplement for current and future environmental issues. The bioremediation using fungi was reported to be more tolerant than bacteria and more efficient for decolorization as well as degradation of toxic chemicals. However, white-rot fungi are well known for their outstanding ability in bioremediation process. Their ability to produce highly non-specific extracellular enzymes allows them to degrade a wide array of pollutants resembling dyes and its derivatives. White-rot fungi secrete one or more of the three principle ligninolytic enzymes: lignin peroxidase (LiP, E.C. 1.11.1.14), Mn-dependent peroxidase (MnP, E.C. 1.11.1.13) and phenol oxidase (laccase) (Lac, E.C. 1.10.3.2) and other peroxidases. The present review discusses comprehensively the science and technology of biodegradation and fungal bioremediation of synthetic dyes.
Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi
Applied and environmental …, 1993
Phanerochaete chrysosporium is rapidly becoming a model system for the study of lignin biodegradation. Numerous studies on the physiology, biochemistry, chemistry, and genetics of this system have been performed. However, P. chrysosporium is not the only fungus to have a lignin-degrading enzyme system. Many other ligninolytic species of fungi, as well as other distantly related organisms which are known to produce lignin peroxidases, are described in this paper. In this study, we demonstrated the presence of the peroxidative enzymes in nine species not previously investigated. The fungi studied produced significant manganese peroxidase activity when they were grown on an oak sawdust substrate supplemented with wheat bran, millet, and sucrose. Many of the fungi also exhibited laccase and/or glyoxal oxidase activity. Inhibitors present in the medium prevented measurement of lignin peroxidase activity. However, Western blots (immunoblots) revealed that several of the fungi produced lignin peroxidase proteins. We concluded from this work that lignindegrading peroxidases are present in nearly all ligninolytic fungi, but may be expressed differentially in different species. Substantial variability exists in the levels and types of ligninolytic enzymes produced by different white rot fungi.
Enzyme and Microbial Technology, 2006
Litter-decomposing basidiomycete fungi (LDF) including environmental isolates from oak forest soil were compared with white-rot fungi for ligninolytic enzymes production and decolorization of synthetic dyes Poly B-411, Reactive Black 5, Reactive Orange 16 and Remazol Brilliant Blue R (RBBR). LDF differed significantly in laccase production. Mycena inclinata and Collybia dryophila produced significant amounts of the enzyme during the whole experiment, while the production in Stropharia rugosoannulata started after 3 weeks of cultivation. Soil isolates exhibited detectable though very low laccase activity. The highest activity of Mn-peroxidase was detected in the cultures of C. dryophila with the peak activities over 30 U l −1 . In all other strains, Mn-peroxidase activity did not exceed 3 U l −1 . The decolorization of 100 mg l −1 dyes after 28 days ranged 80-95% for RBBR, 60-95% for Poly B-411, 58-85% for Reactive Black 5 and 45-82% for Reactive Orange 16. The fastest degradation of Poly B-411 was performed by the strains with high levels of laccase and MnP while the decolorization of other dyes did not depend so strictly on enzyme activities. The highest decolorization of azo dyes was achieved with the LDF C. dryophila, S. rugosoannulata and the soil isolates. The presence of dyes significantly affected enzyme activities in fungal cultures.
Industrial Dye Decolorization by Laccases from Ligninolytic Fungi
Current Microbiology, 1999
White-rot fungi were studied for the decolorization of 23 industrial dyes. Laccase, manganese peroxidase, lignin peroxidase, and aryl alcohol oxidase activities were determined in crude extracts from solid-state cultures of 16 different fungal strains grown on whole oats. All Pleurotus ostreatus strains exhibited high laccase and manganese peroxidase activity, but highest laccase volumetric activity was found in Trametes hispida. Solid-state culture on whole oats showed higher laccase and manganese peroxidase activities compared with growth in a complex liquid medium. Only laccase activity correlated with the decolorization activity of the crude extracts. Two laccase isoenzymes from Trametes hispida were purified, and their decolorization activity was characterized.
2019
Manganese peroxidase (MnP), a crucial enzyme in biodegradation of lignin, is synthesized by most white rot fungi. To obtain novel enzymes with superior biodegradation potential, MnP-producing wild isolates were evaluated for their ability to degrade recalcitrant azo dyes, sulfonephthalein dyes, and kraft lignin. Of 30 wild isolates screened, 18 tested positive for lignin modifying enzymes (LMEs). Thirteen of these isolates were positive for both laccase and MnP, whereas four produced only laccase, and one produced lignin peroxidase alone. The isolates were identified as Clitopilus scyphoides MH172162 (AGUM004), Ganoderma rasinaceum MH172163 (AGUM007), and three Schizophyllum species: MH172164, MH172165, and MH172166 (KONA001, AGUM0011, and AGUM021). The Fourier-transform infrared spectroscopy (FTIR) analysis of dye degradation and kraft lignin samples with AGUM004 and AGUM007 revealed biotransformation. The former could not completely degrade Reactive Black 5 and bromocresol green, ...