scholarly journals Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators.

1992 ◽  
Vol 267 (33) ◽  
pp. 23688-23695 ◽  
Author(s):  
H Wariishi ◽  
K Valli ◽  
M.H. Gold
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Manganese Peroxidase ◽  
Kinetic Mechanism

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 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.

Detailed kinetics of hydrogen abstraction from trans-decalin by OH radicals: the role of hindered internal rotation treatment

2020 ◽  
Vol 22 (44) ◽  
pp. 25740-25746
Author(s):  
Tam V.-T. Mai ◽  
Lam K. Huynh
Keyword(s):  
Master Equation ◽  
Hydrogen Abstraction ◽  
Kinetic Mechanism ◽  
Oh Radicals ◽  
Rate Model ◽  
Wide Range ◽  
Detailed Kinetics ◽  
Kinetics Of ◽  
Detailed Kinetic Mechanism

The detailed kinetic mechanism of the trans-decalin + OH reaction is firstly investigated for a wide range of conditions (T = 200–2000 K & P = 0.76–76000 Torr) using the M06-2X/aug-cc-pVTZ level and stochastic RRKM-based Master equation rate model.

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