scholarly journals Production of Ligninolytic Enzymes by White-Rot FungusDatroniasp. KAPI0039 and Their Application for Reactive Dye Removal

2010 ◽  
Vol 2010 ◽  
pp. 1-6 ◽  
Author(s):  
Pilanee Vaithanomsat ◽  
Waraporn Apiwatanapiwat ◽  
Oncheera Petchoy ◽  
Jirawate Chedchant

This study focused on decolorization of 2 reactive dyes; Reactive Blue 19 (RBBR) and Reactive Black 5 (RB5), by selected white-rot fungusDatroniasp. KAPI0039. The effects of reactive dye concentration, fungal inoculum size as well as pH were studied. Samples were periodically collected for the measurement of color unit, Laccase (Lac), Manganese Peroxidase (MnP), and Lignin Peroxidase (LiP) activity. Eighty-six percent of 1,000 mg L−1RBBR decolorization was achieved by 2% (w/v)Datroniasp. KAPI0039 at pH 5. The highest Lac activity (759.81 UL−1) was detected in the optimal condition. For RB5,Datroniasp. KAPI0039 efficiently performed (88.01% decolorization) at 2% (w/v) fungal inoculum size for the reduction of 600 mg L−1RB5 under pH 5. The highest Lac activity (178.57 UL−1) was detected, whereas the activity of MnP and LiP was absent during this hour. The result, therefore, indicated thatDatroniasp. KAPI0039 was obviously able to breakdown both reactive dyes, and Lac was considered as a major lignin-degradation enzyme in this reaction.

2020 ◽  
Author(s):  
Jianqiao Wang ◽  
Tomohiro Suzuki ◽  
Hideo Dohra ◽  
Toshio Mori ◽  
Hirokazu Kawagishi ◽  
...  

Abstract Background Lignocellulosic biomass is an organic matrix composed of cellulose, hemicellulose, and lignin. In nature, lignin degradation by basidiomycetes is the key step in lignocellulose decay. The white-rot fungus Phanerochaete sordida YK-624 (YK-624) has been extensively studied due to its high lignin degradation ability. In our previous study, it was demonstrated that YK-624 can secrete lignin peroxidase and manganese peroxidase for lignin degradation. However, the underlying mechanism for lignin degradation by YK-624 remains unknown.Results Here, we analyzed YK-624 gene expression following growth under ligninolytic and nonligninolytic conditions and compared the differentially expressed genes in YK-624 to those in the model white-rot fungus P. chrysosporium by next-generation sequencing. More ligninolytic enzymes and lignin-degrading auxiliary enzymes were upregulated in YK-624. This might explain the high degradation efficiency of YK-624. In addition, the genes involved in energy metabolism pathways, such as the TCA cycle, oxidative phosphorylation, lipid metabolism, carbon metabolism and glycolysis, were upregulated under ligninolytic conditions in YK-624.Conclusions In the present study, the first differential gene expression analysis of YK-624 under ligninolytic and nonligninolytic conditions was reported. The results obtained in this study indicated that YK-624 produces more energy- and lignin-degrading enzymes for more efficient lignin biodegradation.


1998 ◽  
Vol 44 (7) ◽  
pp. 676-680 ◽  
Author(s):  
Orly Ardon ◽  
Zohar Kerem ◽  
Yitzhak Hadar

The white rot fungus Pleurotus ostreatus was grown in a chemically defined solid state fermentation system amended with cotton stalk extract (CSE).Treated cultures exhibited increased laccase activity as well as enhanced lignin mineralization. Mineralization of [14C]lignin initialized 4 days earlier in CSE-supplemented cultures than in control cultures. Total mineralization in the first 16 days was 15% in the CSE-treated cultures, compared with only 7% in the controls. Cotton stalk extract also contained compounds that serve as substrates for laccase purified from P. ostreatus as shown by oxygen consumption, as well as changes in the UV–visible spectrum.Key words: cotton, Pleurotusostreatus, white rot, laccase, lignin biodegradation.


2017 ◽  
pp. 265-275
Author(s):  
B. S. Shanthi Kumari ◽  
Kanderi Dileep Kumar ◽  
K. Y. Usha ◽  
A. Ramya ◽  
B. Rajasekhar Reddy

Molecules ◽  
2019 ◽  
Vol 24 (21) ◽  
pp. 3914 ◽  
Author(s):  
Peng Qin ◽  
Yuetong Wu ◽  
Bilal Adil ◽  
Jie Wang ◽  
Yunfu Gu ◽  
...  

Many dyes and pigments are used in textile and printing industries, and their wastewater has been classed as a top source of pollution. Biodegradation of dyes by fungal laccase has great potential. In this work, the influence of reaction time, pH, temperature, dye concentration, metal ions, and mediators on laccase-catalyzed Remazol Brilliant Blue R dye (RBBR) decolorization were investigated in vitro using crude laccase from the white-rot fungus Ganoderma lucidum. The optimal decolorization percentage (50.3%) was achieved at 35 °C, pH 4.0, and 200 ppm RBBR in 30 min. The mediator effects from syringaldehyde, 1-hydroxybenzotriazole, and vanillin were compared, and 0.1 mM vanillin was found to obviously increase the decolorization percentage of RBBR to 98.7%. Laccase-mediated decolorization percentages significantly increased in the presence of 5 mM Na+ and Cu2+, and decolorization percentages reached 62.4% and 62.2%, respectively. Real-time fluorescence-quantitative PCR (RT-PCR) and protein mass spectrometry results showed that among the 15 laccase isoenzyme genes, Glac1 was the main laccase-contributing gene, contributing the most to the laccase enzyme activity and decolorization process. These results also indicate that under optimal conditions, G. lucidum laccases, especially Glac1, have a strong potential to remove RBBR from reactive dye effluent.


Evidence in support of an essential role for H 2 O 2 in lignin degradation by the white-rot fungus Phanerochaete chrysosporium has been presented by several laboratories. H 2 O 2 is formed simultaneously with the ligninolytic system, and when it is degraded by catalase the lignin-degrading capacity is also reduced. We have now identified, purified and characterized a sugar-oxidizing enzyme that produces H 2 O 2 during glucose starvation in P. chrysosporium . The enzyme oxidizes glucose at the 2-carbon position to yield glucosone, but 5-n-gluconolactone and xylose are also oxidized at significant rates. Another H 2 O 2 -producing enzyme in P.chrysosporium , methanol oxidase, has also been identified, purified and characterized in this laboratory. Methanol is formed from the methoxyl groups in lignin. Hydrogen peroxide, necessary for further degradation of lignin, is formed by enzyme-catalysed oxidation of the lignin-derived methanol. Induction and repression of the H 2 O 2 -producing enzymes is discussed, as well as ways for the fungus to control the glucose level in its environment.


1994 ◽  
Vol 32 (3) ◽  
pp. 299-307 ◽  
Author(s):  
A.A. Leontievsky ◽  
N.M. Myasoedova ◽  
L.A. Golovleva

2006 ◽  
Vol 1 (3) ◽  
Author(s):  
Dawen Gao ◽  
Xianghua Wen ◽  
Yonggang Zeng ◽  
Yi Qian

Most studies on decolourization of reactive dye with Phanerochaete chrysosporium have been performed under sterile conditions. In this paper, Phanerochaete chrysosporium, suspended in liquid medium, immobilized on nylon nets, and immobilized on polyurethane foams were studied to decolorize a textile-reactive dye in agitated liquid incubation under non-sterile conditions. The results showed that the decolourization against reactive brilliant red K-2BP by mycelia pellets in suspended cultures, the fungi immobilized on nylon nets and immobilized on polyurethane foams were 0%, 52% and 95%, respectively. The suspended incubation system and the system with nylon nets were contaminated with yeasts, which deteriorated the decolourization effects. The three-dimensional reticular structure of polyurethane foam was benefit to Phanerochaete chrysosporium growth in spreading mycelia taking nutrients and oxygen effectively. The foam could quickly absorb liquid medium into its holes, leaving much less nutrients to support the growth of single cell micro-organisms such as yeast in liquid. The micro-environment existed in polyurethane foam was close to the wild growth conditions of white rot fungus in nature. In conclusion, immobilized culture with polyurethane foam carriers is advantaged to reduce the colonization of other micro-organisms, and makes Phanerochaete chrysosporium possess higher decolorizing ability under non-sterile conditions.


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