scholarly journals Phenanthrene Removal from Soil by a Strain of Aspergillus niger Producing Manganese Peroxidase of Phanerochaete chrysosporium

Hydrocarbon ◽  
10.5772/51944 ◽  
2013 ◽  
Author(s):  
Diana V. ◽  
Angel E.
Keyword(s):  
Aspergillus Niger ◽  
Phanerochaete Chrysosporium ◽  
Manganese Peroxidase

scholarly journals Calnexin Overexpression Increases Manganese Peroxidase Production in Aspergillus niger

2002 ◽  
Vol 68 (2) ◽  
pp. 846-851 ◽  
Author(s):  
Ana Conesa ◽  
David Jeenes ◽  
David B. Archer ◽  
Cees A. M. J. J. van den Hondel ◽  
Peter J. Punt
Keyword(s):  
Aspergillus Niger ◽  
Synergistic Effect ◽  
Phanerochaete Chrysosporium ◽  
Manganese Peroxidase ◽  
Culture Medium ◽  
White Rot ◽  
Expression Level ◽  
Prosthetic Group ◽  
Secretion Pathway

ABSTRACT Heme-containing peroxidases from white rot basidiomycetes, in contrast to most proteins of fungal origin, are poorly produced in industrial filamentous fungal strains. Factors limiting peroxidase production are believed to operate at the posttranslational level. In particular, insufficient availability of the prosthetic group which is required for peroxidase biosynthesis has been proposed to be an important bottleneck. In this work, we analyzed the role of two components of the secretion pathway, the chaperones calnexin and binding protein (BiP), in the production of a fungal peroxidase. Expression of the Phanerochaete chrysosporium manganese peroxidase (MnP) in Aspergillus niger resulted in an increase in the expression level of the clxA and bipA genes. In a heme-supplemented medium, where MnP was shown to be overproduced to higher levels, induction of clxA and bipA was also higher. Overexpression of these two chaperones in an MnP-producing strain was analyzed for its effect on MnP production. Whereas bipA overexpression seriously reduced MnP production, overexpression of calnexin resulted in a four- to fivefold increase in the extracellular MnP levels. However, when additional heme was provided in the culture medium, calnexin overexpression had no synergistic effect on MnP production. The possible function of these two chaperones in MnP maturation and production is discussed.

scholarly journals Manganese Peroxidase from the Lignin-degrading Basidiomycete Phanerochaete chrysosporium

1989 ◽  
Vol 264 (6) ◽  
pp. 3335-3340 ◽  
Author(s):  
H Wariishi ◽  
H B Dunford ◽  
I D MacDonald ◽  
M H Gold
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Manganese Peroxidase

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

Biologia ◽  
2014 ◽  
Vol 69 (11) ◽  
Author(s):  
Denisse González-Ramírez ◽  
Claudia Muro-Urista ◽  
Ainhoa Arana-Cuenca ◽  
Alejandro Téllez-Jurado ◽  
Aldo González-Becerra
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Peroxidase Activity ◽  
Manganese Peroxidase ◽  
Enzyme Production ◽  
Laccase Activity ◽  
Alginate Beads ◽  
Airlift Reactor ◽  
Airlift Bioreactor ◽  
Brilliant Blue ◽  
Maximum Percentage

AbstractEnzyme production by immobilized Phanerochaete chrysosporium was evaluated in airlift bioreactor and agitated cultures. Free mycelium and immobilized mycelium on alginate beads were tested in the decolourization of 50 and 500 mg/L of Remazol Brilliant Blue R. Dye concentration did not inhibit the fungi development in all tests. In addition, high decolourization percentage of dye was found with free mycelium (99%) in agitated flasks and with immobilized mycelium in airlift (98%). However, decolourization period by immobilized mycelium (120 h) was greater than that by the free mycelium (14 h). Important manganese peroxidase, lignine peroxidase and laccase activities were identified in decolourization process. Manganese peroxidase appeared to be promoted by high dye concentrations during the treatment with immobilized mycelium, but this enzyme was not detected with free mycelium in airlift. Bioreactor prompted also laccase and lignine peroxidase actions in both tests; free mycelium registered a maximum laccase action of 31.569 × 103 U/L in 70 h, whereas immobilized mycelium registered 1.680 × 103 U/L in 170 h, while lignine peroxidase secretion by free P. chrysosporium was higher (1.300 × 103 U/L) than immobilized mycelium (1.250 × 103 U/L). Maximum laccase activity coincided with the maximum percentage of decolourization, however, high peroxidase activity was identified from the start of dye treatment.

scholarly journals Congo Red Decolorization and Detoxification by Aspergillus niger: Removal Mechanisms and Dye Degradation Pathway

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Nedra Asses ◽  
Lamia Ayed ◽  
Neila Hkiri ◽  
Moktar Hamdi
Keyword(s):  
Molecular Structure ◽  
Aspergillus Niger ◽  
Azo Dyes ◽  
Lignin Peroxidase ◽  
Congo Red ◽  
Manganese Peroxidase ◽  
Dye Degradation ◽  
Degradation Pathway ◽  
Effects Of Ph ◽  
Maximum Decolorization

Congo red is one of the best known and used azo dyes which has two azo bonds (-N=N-) chromophore in its molecular structure. Its structural stability makes it highly toxic and resistant to biodegradation. The objective of this study was to assess the congo red biodegradation and detoxification by Aspergillus niger. The effects of pH, initial dye concentration, temperature, and shaking speed on the decolorization rate and enzymes production were studied. The maximum decolorization was correlated with lignin peroxidase and manganese peroxidase production. Above 97% were obtained when 2 g mycelia were incubated at pH 5, in presence of 200 mg/L of dye during 6 days at 28°C and under 120 to 150 rpm shaking speed. The degraded metabolites were characterized by using LC-MS/MS analyses and the biodegradation mechanism was also studied. Congo red bioconversion formed degradation metabolites mainly by peroxidases activities, i.e., the sodium naphthalene sulfonate (m/z = 227) and the cycloheptadienylium (m/z = 91). Phytotoxicity and microtoxicity tests confirmed that degradation metabolites were less toxic than original dye.

scholarly journals Effects of supplementation with phosphorus, calcium and manganese during oil palm frond fermentation by Phanerochaete chrysosporium on ligninase enzyme activity

2020 ◽  
Vol 21 (5) ◽  
Author(s):  
Roni Pazla ◽  
Novirman Jamarun ◽  
Fauzia Agustin ◽  
Mardiati Zain ◽  
Arief Arief ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Phanerochaete Chrysosporium ◽  
Oil Palm ◽  
Manganese Peroxidase ◽  
Crude Protein ◽  
Lignin Degradation ◽  
Lignin Content ◽  
Oil Palm Frond ◽  
Range Test ◽  
Palm Frond

Abstract. Pazla R, Jamarun N, Agustin F, Zain M, Cahyani NO. 2020. Effects of supplementation with phosphorus, calcium and manganese during oil palm frond fermentation by Phanerochaete chrysosporium on ligninase enzyme activity. Biodiversitas 21: 1833-1838. The objective of this study was to evaluate the effects of supplementation with phosphorus (P) in combination with calcium (Ca) and manganese (Mn) during oil palm frond (OPF) fermentation by Phanerochaete chrysosporium on ligninase enzyme activity and lignin degradation. This study was carried out using a randomized complete design with 3 treatments (addition of P, Ca and Mn) and 5 replicates. The following treatments were performed: T1 (P 1000 + Ca 2000 + Mn 150 ppm), T2 (P 1500 + Ca 2000 + Mn 150 ppm), and T3  (P 2000 + Ca 2000 +Mn 150 ppm). The data were subjected to an analysis of variance (ANOVA), and differences between treatment means were tested using Duncan's multiple range test (DMRT). The parameters measured were as follows: lignin peroxidase (LiP) activity (U/mL), manganese peroxidase (MnP) activity (U/mL), crude protein (CP) content (%), crude fiber (CF) content (%) and the decrease in lignin (%). The results revealed a significant increase in LiP activity and CP content and a decrease in the lignin content (p<0.05) by the addition of P in the T3 treatment. However, the treatment nonsignificantly increased (p>0.05) MnP activity and significantly decreased (P<0.05) the CF content. In conclusion, supplementation of the OPF fermentation process with P 2000, Ca 2000, and Mn 150 ppm resulted in the highest ligninase enzyme activity and in decreased lignin content.

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+.

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