scholarly journals Side-by-side biochemical comparison of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare on their activity against crystalline cellulose and glucomannan

PLoS ONE ◽  
2018 ◽  
Vol 13 (9) ◽  
pp. e0203430 ◽  
Author(s):  
Bing Liu ◽  
Sumitha Krishnaswamyreddy ◽  
Madhu Nair Muraleedharan ◽  
Åke Olson ◽  
Anders Broberg ◽  
...  
2012 ◽  
Vol 95 (4) ◽  
pp. 979-990 ◽  
Author(s):  
Igor Yakovlev ◽  
Gustav Vaaje-Kolstad ◽  
Ari M. Hietala ◽  
Emil Stefańczyk ◽  
Halvor Solheim ◽  
...  

2020 ◽  
Vol 49 (11) ◽  
pp. 3413-3422 ◽  
Author(s):  
Luisa Ciano ◽  
Alessandro Paradisi ◽  
Glyn R. Hemsworth ◽  
Morten Tovborg ◽  
Gideon J. Davies ◽  
...  

Semi-orientated EPR spectroscopy reveals that lytic polysaccharide monooxygenases interact with their natural cellulose substrate in a specific way, where the copper active site is positioned adjacent to the edge of a crystalline cellulose fibril.


Author(s):  
Mikako Tachioka ◽  
Akihiko Nakamura ◽  
Takuya Ishida ◽  
Kiyohiko Igarashi ◽  
Masahiro Samejima

Cellobiohydrolases belonging to glycoside hydrolase family 6 (CBH II, Cel6A) play key roles in the hydrolysis of crystalline cellulose. CBH II from the white-rot fungusPhanerochaete chrysosporium(PcCel6A) consists of a catalytic domain (CD) and a carbohydrate-binding module connected by a linker peptide, like other known fungal cellobiohydrolases. In the present study, the CD ofPcCel6A was crystallized without ligands, andp-nitrophenyl β-D-cellotrioside (pNPG3) was soaked into the crystals. The determined structures of the ligand-free andpNPG3-soaked crystals revealed that binding of cellobiose at substrate subsites +1 and +2 induces a conformational change of the N-terminal and C-terminal loops, switching the tunnel-shaped active site from the open to the closed form.


2012 ◽  
Vol 3 (1) ◽  
pp. 20-21
Author(s):  
A.Sangeetha A.Sangeetha ◽  
◽  
K.Thanigai K.Thanigai ◽  
Narasimhamurthy Narasimhamurthy ◽  
S.K.Nath S.K.Nath

2020 ◽  
Vol 93 (9) ◽  
pp. 289-292
Author(s):  
Yumi SHIMIZU ◽  
Shuma SATHO ◽  
Taro NAKAJIMA ◽  
Hiroaki KOUZAI ◽  
Kiminori SHIMIZU

2018 ◽  
Vol 69 (1) ◽  
pp. 38-44
Author(s):  
Nicoleta Mirela Marin ◽  
Olga Tiron ◽  
Luoana Florentina Pascu ◽  
Mihaela Costache ◽  
Mihai Nita Lazar ◽  
...  

This study investigates the synergistic effects of ion exchange and biodegradation methods to remove the Acid Blue 193 also called Gryfalan Navy Blue RL (GNB) dye from wastewater. Ion exchange studies were performed using a strongly basic anion exchange resin Amberlite IRA 400. The equilibrium was characterized by a kinetic and thermodynamic points of view, establishing that the sorption of the GNB dye was subject to the Freundlich isotherm model with R2 = 0.8710. Experimental results showed that the activated resin can removed up to 93.4% when the concentration of dye solution is 5.62�10-2 mM. The biodegradation of the GNB was induced by laccase, an enzyme isolated from white-rot fungus. It was also analyzed the role of pH and dye concentration on GNB biodegradation, so 5�10-2 mM dye had a maximum discoloration efficiency of 82.9% at pH of 4. The laccase showed a very fast and robust activity reaching in a few minutes a Km value of 2.2�10-1mM. In addition, increasing the GNB concentration up to 8�10-1 mM did not triggered a substrat inhibition effect on the laccase activity. Overall, in this study we proposed a mixt physicochemical and biological approach to enhance the GNB removal and biodegradability from the wastewaters and subsequently the environment.


1991 ◽  
Vol 24 (3-4) ◽  
pp. 189-198 ◽  
Author(s):  
V. P. Lankinen ◽  
M. M. Inkeröinen ◽  
J. Pellinen ◽  
A. I. Hatakka

Decrease of adsorbable organic chlorine (AOX) is becoming the most important criterion for the efficiency of pulp mill effluent treatment in the 1990s. Two methods, designated MYCOR and MYCOPOR which utilize the white-rot fungus Phanerochaete chrysosporium have earlier been developed for the color removal of pulp mill effluents, but the processes have also a capacity to decrease the amount of chlorinated organic compounds. Lignin peroxidases (ligninases) produced by P. chrvsosporium may dechlorinate chlorinated phenols. In this work possibilities to use selected white-rot fungi in the treatment of E1-stage bleach plant effluent were studied. Phlebia radiata. Phanerochaete chrvsosporium and Merulius (Phlebia) tremellosus were compared in shake flasks for their ability to produce laccase, lignin peroxidase(s) and manganese-dependent peroxidase(s) and to remove color from a medium containing effluent. Softwood bleaching effluents were treated by carrier-immobilized P. radiata in 2 1 bioreactors and a 10 1 BiostatR -fermentor. Dechlorination was followed using Cl ion and AOX determinations. All fungi removed the color of the effluent. In P. radiata cultivations AOX decrease was ca. 4 mg l−1 in one day. Apparent lignin peroxidase activities as determined by veratryl alcohol oxidation method were negligible or zero in a medium with AOX content of ca. 60 mg l−1, prepared using about 20 % (v/v) of softwood effluent. However, the purification of extracellular enzymes implied that large amounts of lignin peroxidases were present in the medium and, after the purification, in active form. Enzyme proteins were separated using anion exchange chromatography, and they were further characterized by electrophoresis (SDS-PAGE) to reveal the kind of enzymes that were present during AOX decrease and color removal. The most characteristic lignin peroxidase isoenzymes in effluent media were LiP2 and LiP3.


Sign in / Sign up

Export Citation Format

Share Document