Differential expression of manganese peroxidase and laccase in white-rot fungi in the presence of manganese or aromatic compounds

2000 ◽  
Vol 54 (5) ◽  
pp. 686-691 ◽  
Author(s):  
T. Scheel ◽  
M. Höfer ◽  
S. Ludwig ◽  
U. Hölker
Keyword(s):  
Differential Expression ◽  
Aromatic Compounds ◽  
Manganese Peroxidase ◽  
White Rot Fungi ◽  
White Rot

Effect of aromatic compounds on growth and ligninolytic enzyme production of two white rot fungi Ceriporiopsis subvermispora and Cyathus stercoreus

1998 ◽  
Vol 44 (9) ◽  
pp. 872-885 ◽  
Author(s):  
Anand Sethuraman ◽  
Danny E Akin ◽  
Jason G Eisele ◽  
Karl-Erik L Eriksson
Keyword(s):  
Cinnamic Acid ◽  
Aromatic Compounds ◽  
Manganese Peroxidase ◽  
Enzyme Production ◽  
White Rot Fungi ◽  
Hyphal Growth ◽  
White Rot ◽  
Ceriporiopsis Subvermispora ◽  
Cyathus Stercoreus ◽  
Benzaldehyde Derivatives

Seven benzoic acid, ten cinnamic acid, and five benzaldehyde derivatives were tested for their effects on hyphal growth and production of laccase and manganese peroxidase by Ceriporiopsis subvermispora FP 90031-sp and Cyathus stercoreus ATCC 36910. Derivatives tested included phenolic compounds and their corresponding unsubstituted and O-methylated derivatives. Benzaldehyde derivatives were more toxic to both fungi than the corresponding benzoic and cinnamic acid derivatives. Hyphal growth was generally increased at a low concentration of 1 mM, while higher concentrations of 5-10 mM mostly resulted in less or no growth. Hyphal growth and enzyme production response were compound specific. However, generally monomethoxylated compounds were more toxic than compounds with an additional methoxyl group. Cyathus stercoreus was more sensitive than Ceriporiopsis subvermispora to most of the compounds tested and thus showed poorer growth. Cyathus stercoreus produced higher concentrations of manganese peroxidase than Ceriporiopsis subvermispora for all the compounds tested, whereas laccase activity was higher in Ceriporiopsis subvermispora for most of the compounds tested. Di- and tri-methoxylated compounds induced more laccase and manganese peroxidase activities than the corresponding hydroxylated derivatives. At 1 mM levels, 3,4-dimethoxycinnamic acid induced the greatest increase in laccase production for Ceriporiopsis subvermispora and Cyathus stercoreus (245 and 290% of control, respectively). Syringic acid induced manganese peroxidase (MnP) to 536% of that in control for Ceriporiopsis subvermispora, and both 3,4-dimethoxycinnamic acid and 3,4,5-trimethoxycinnamic acid induced MnP to over 300% of control for Cyathus stercoreus. The results provide a body of information on the effects of specific aromatic compounds on two potentially industrially important fungi. Key words: biomass conversion, aromatic compounds, white rot fungi, fungal growth, enzyme production.

Production of laccase and manganese peroxidase by white-rot fungi from sugarcane bagasse in solid bed: Use for dyes decolourisation

Sugar Tech ◽  
2008 ◽  
Vol 10 (3) ◽  
pp. 260-264 ◽  
Author(s):  
Gilda Guerra ◽  
Osmel Domínguez ◽  
Miguel Ramos-Leal ◽  
Ana M. Manzano ◽  
María I. Sánchez ◽  
...  
Keyword(s):  
Sugarcane Bagasse ◽  
Manganese Peroxidase ◽  
White Rot Fungi ◽  
White Rot

scholarly journals Functional Expression and One-Step Protein Purification of Manganese Peroxidase 1 (rMnP1) from Phanerochaete chrysosporium Using the E. coli-Expression System

2020 ◽  
Vol 21 (2) ◽  
pp. 416
Author(s):  
Angel De La Cruz Pech-Canul ◽  
Javier Carrillo-Campos ◽  
María de Lourdes Ballinas-Casarrubias ◽  
Rosa Lidia Solis-Oviedo ◽  
Selena Karina Hernández-Rascón ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Protein Purification ◽  
Phanerochaete Chrysosporium ◽  
Manganese Peroxidase ◽  
Expression System ◽  
White Rot Fungi ◽  
Functional Expression ◽  
White Rot ◽  
E Coli ◽  
One Step

Manganese peroxidases (MnP) from the white-rot fungi Phanerochaete chrysosporium catalyse the oxidation of Mn2+ to Mn3+, a strong oxidizer able to oxidize a wide variety of organic compounds. Different approaches have been used to unravel the enzymatic properties and potential applications of MnP. However, these efforts have been hampered by the limited production of native MnP by fungi. Heterologous expression of MnP has been achieved in both eukaryotic and prokaryotic expression systems, although with limited production and many disadvantages in the process. Here we described a novel molecular approach for the expression and purification of manganese peroxidase isoform 1 (MnP1) from P. chrysosporium using an E. coli-expression system. The proposed strategy involved the codon optimization and chemical synthesis of the MnP1 gene for optimised expression in the E. coli T7 shuffle host. Recombinant MnP1 (rMnP1) was expressed as a fusion protein, which was recovered from solubilised inclusion bodies. rMnP1 was purified from the fusion protein using intein-based protein purification techniques and a one-step affinity chromatography. The designated strategy allowed production of an active enzyme able to oxidize guaiacol or Mn2+.

Large scale production of manganese-peroxidase using agaric white-rot fungi

2002 ◽  
Vol 30 (4) ◽  
pp. 556-561 ◽  
Author(s):  
J. Nüske ◽  
K. Scheibner ◽  
U. Dornberger ◽  
R. Ullrich ◽  
M. Hofrichter
Keyword(s):  
Manganese Peroxidase ◽  
Large Scale ◽  
White Rot Fungi ◽  
White Rot ◽  
Scale Production ◽  
Large Scale Production

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.

scholarly journals A novel Versatile Peroxidase from Lentinus squarrosulus (MH172167)towards enhanced delignification and digestibility of crop residues

2018 ◽  
Author(s):  
R Aarthi ◽  
Ramya G Rao ◽  
Vandana Thammaiah ◽  
SM Gopinath ◽  
Manpal Sridhar
Keyword(s):  
Solid State ◽  
Peroxidase Activity ◽  
Aromatic Compounds ◽  
Submerged Fermentation ◽  
Crop Residues ◽  
White Rot Fungi ◽  
Neutral Detergent Fiber ◽  
White Rot ◽  
Versatile Peroxidase ◽  
Livestock Productivity

AbstractScarcity of quality feed is a major constraint concerning livestock productivity with recalcitrant lignin hindering utilization of crop residues as quality animal feed. Degradation of lignin in nature is contributed by white-rot fungi through their enriched ligninolytic system. Versatile Peroxidase plays a key role in ligninolysis through its capability to oxidize diverse class of aromatics without mediators. In this study, wild isolates of wood rotting fungi were screened for potential peroxidases oxidizing manganese and aromatic compounds. The strain identified asLentinus squarrosulus(TAMI004, BankIt2098576 MH172167) was monitored for enzyme activity in solid state and submerged fermentation.L. squarrosulusdemonstrated predominant Versatile Peroxidase activity amongst the screened wild isolates displaying hybrid characteristic of manganese oxidation and manganese independent reactions on aromatic compounds. The manganese oxidizing peroxidase activity evidenced in submerged fermentation was 12 IU/L whereas in solid state fermentation it was 131 IU/L. This ability to act through manganese mediated and independent reactions on phenolics reveals its biotechnological and industrial significance. Treatment of common crop residues with crude extract ofL. squarrosulusrich in Versatile Peroxidase obtained from both Solid state and submerged fermentations showed a decrease in their Neutral Detergent Fiber, Acid Detergent Fiber and Acid Detergent Lignin content showing biodegradation, substantiating the ligninolytic ability and more prominently increase in their digestibility. To the best of our knowledge, this is the first report describing Versatile Peroxidase fromLentinus squarrosuluswith potential to augment the ruminant digestibility of crop residues.ImportanceVersatile Peroxidase of White-rot fungi, a relatively less studied lignolytic enzyme, is very efficient in depolymerization of lignin macromolecule through its multivalent catalytic sites. Lignin degradation is very appealing from the application perspective as attack on lignin exposes the energy affluent polysaccharides for utilization in extensive biotechnological applications. Reports on relevance of Versatile Peroxidase for these purposes are still emerging, however the role of ligninolytic enzymes especially Versatile Peroxidase in enriching ruminant feed is yet unturned. Here, this work demonstrates the potential of Versatile Peroxidase from a novel speciesLentinus squarrosulusin delignification thereby upgrading the digestibility and nutritive value of crop residues. The observations validate the importance of the enzyme in improvement of crop residues for feeding ruminants in the current scenario where, livestock productivity is severely impacted by lack of quality feed and demand for alternate feed resources is intensifying.

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