Optimum stability conditions of pH and temperature for ligninase and manganese-dependent peroxidase from Phanerochaete chrysosporium. Application to in vitro decolorization of Poly R-478 by MnP

Couto, Susana Rodrı́guez; Moldes, Diego; Sanromán, M. Ángeles

doi:10.1007/s11274-005-9078-0

Cited by 36 publications

(18 citation statements)

References 28 publications

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“…The optimum pH for LiP activity is 4.2. LiP is stable at 34ÚC and pH 4.2 for 100 h (Couto et al, 2006). Therefore, it seems that succinate buffer is able to supply the optimum pH for Lip activity and stability rather than acetate buffer.…”

Section: Resultsmentioning

confidence: 99%

Decolorization of different azo dyes by Phanerochaete chrysosporium RP78 under optimal condition

Ghasemi

Tabandeh

Bambai

et al. 2010

Int. J. Environ. Sci. Technol.

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ABSTRACT:Detoxification of synthetic dyes is one of the main challenges in clearing textile industry wastes.Biodegradation of azo-dyes using Phanerochaete chrysosporium is one the most environmentally friendly methods available. The main enzymes responsible for mycodecolorization process are lignin and manganese peroxidases. Here, optimization of expression conditions has been carried out with manipulating culture condition and nutrient sources. Therefore, the effects of buffer and temperature as well as nitrogen source on lignin peroxidase and manganese peroxidase production were investigated at two levels and four levels, respectively. For this purpose, P. chrysosporium RP78 based on Taguchi design of experiment has been applied. Maximum lignin and manganese peroxidase activities of 182 ± 2.5 U/L and 850 ± 41 U/L were obtained under predicted optimum conditions, respectively. Thereby, about 100 % decolorization was achieved after 24 h for two most widely used groups of azo dyes in textile industry consisting reactive and acidic. The physical adsorption of the azo dyes by mycelia was not significant which indicated that the enzymatic degradation of the dyes was occurred. Time profile of these enzymes showed that manganese peroxidase was peaked on 9 th day while lignin peroxidase peaked on 13 th. day and remained stable in the culture. The extracellular expression profiles of both were studied by 2 dimensional gel electrophoresis to partially characterize the enzymes.

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Section: Resultsmentioning

confidence: 99%

Decolorization of different azo dyes by Phanerochaete chrysosporium RP78 under optimal condition

Ghasemi

Tabandeh

Bambai

et al. 2010

Int. J. Environ. Sci. Technol.

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“…The LiP activity dropped more than 75% at temperatures below 35°C and lost about 66% of its activity at a temperature of 75°C. Other authors found the LiP enzyme to have an optimum stable temperature of 34°C [45]. Bosco et al [46] found that a mixture of LiP isoenzymes from immobilized cultures of P. chrysosporium catalyzed oxidation reactions at acidic pH and temperatures between 25 and 60°C.…”

Section: Resultsmentioning

confidence: 99%

“…More than 70% of activity was lost at pH 7-11. Couto et al [45] studied the stability of LiP enzyme produced by P. chrysosporium and found an optimum pH of 4.2. Other authors have made similar observations [46].…”

Section: Resultsmentioning

confidence: 99%

Optimization of lignin peroxidase production and stability by Phanerochaete chrysosporium using sewage-treatment-plant sludge as substrate in a stirred-tank bioreactor

Alam

Mansor

Jalal

2009

J Ind Microbiol Biotechnol

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A laboratory-scale study was carried out to produce lignin peroxidase (ligninase) by white rot fungus (Phanerochaete chrysosporium) using sewage-treatment-plant (STP) sludge as the major substrate. The optimization was done using full-factorial design (FFD) with agitation and aeration as the two parameters. Nine experiments indicated by the FFD were fermented in a stirred-tank bioreactor for 3 days. A second-order quadratic model was developed using the regression analysis of the experimental results with the linear, quadratic, and interaction effects of the parameters. Analysis of variance (ANOVA) showed a high coefficient of determination (R (2)) value of 0.972, thus indicating a satisfactory fit of the quadratic model with the experimental data. Using statistical analysis, the optimum aeration and agitation rates were determined to be 2.0 vvm and 200 rpm, respectively, with a maximum activity of 225 U l(-1) in the first 3 days of fermentation. The validation experiment showed the maximum activity of lignin peroxidase was 744 U l(-1) after 5 days of fermentation. The results for the tests of the stability of lignin peroxidase showed that the activity was more than 80% of the maximum for the first 12 h of incubation at an optimum pH of 5 and temperature of 55 degrees C.

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“…POXs from both A. viscosus and A. israelii were very stable between pH 6.0 and 8.0 exhibiting maximum stability at pH 7.0 with 64% and 77% relative residual activity at pH 6.0 and 8.0, respectively (Figure 1(b)). Rodrıguez-Couto et al [28] reported POXs from white rot fungus, Phanerochaete chrysosporium which exhibited great stability only at pH around 4.5. Also, POX from Pleurotus sajor caju MTCC-141 was stable and active around pH 3.0 [29].…”

Section: Effect Of Ph On Total Pox Activity and Stabilitymentioning

confidence: 99%

“…In another report, POX from the white-rot fungus, Irpex lacteus showed high stability between 30˚C and 40˚C [32]. Rodríguez-Couto et al [28] reported POXs from P. chrysosporium which were most stable between 32˚C and 34˚C. High thermostability is an attractive and desirable characteristic of an enzyme for a variety of industrial and biotechnological applications [33]- [35].…”

Section: Effect Of Temperature On Total Pox Activity and Stabilitymentioning

confidence: 99%

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Olajuyigbe¹,

Ehiosun²,

Jaiyesimi³

2015

AER

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Peroxidases (POXs) are the key extracellular enzymes produced by crude oil degrading microbes. Knowledge of optimum conditions for POXs activity is crucial for providing effective environment for bioremediation. In this study, physicochemical properties of POXs produced by Actinomyces israelii and Actinomyces viscosus during growth on crude oil were studied. The POXs exhibited similarities in activity and stability with striking differences in response to two divalent metal ions. The POXs from both species had optimum pH of 7.0 and were very stable over a narrow pH range (6.0 -8.0). The POXs demonstrated similar thermostability exhibiting relative residual activity of 62% at 50˚C after 30 min incubation and 45% residual activity at the same temperature after 60 min despite the fact that POXs from A. viscosus and A. israelii had optimum temperatures of 50˚C and 40˚C, respectively. The POXs from A. viscosus and A. israelii were greatly activated by Fe 2+ at 5.0 and 10.0 mM. The enzymes were both strongly inhibited by Cu 2+ , Mg 2+ and Hg 2+ . Surprisingly, these congeneric POXs demonstrated striking differences in their response to Ca 2+ and Mn 2+ . POX from A. viscosus was activated by Ca 2+ and Mn 2+ exhibiting relative activity of 136% and 106% at 5 mM, respectively. In contrast, POX from A. israelii was strongly inhibited by Ca 2+ and Mn 2+ exhibiting 62.5% relative activity in the presence of 5 mM of each metal ion. Increasing the concentration of Ca 2+ and Mn 2+ led to further activation of POX from A. viscosus and inhibition of POX from A. israelii. Results provide deeper insights into functional properties of studied POXs from closely related microbes. The physicochemical properties are very similar; however, notable differences provide a strong basis for structural characterization of these congeneric enzymes.

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Optimum stability conditions of pH and temperature for ligninase and manganese-dependent peroxidase from Phanerochaete chrysosporium. Application to in vitro decolorization of Poly R-478 by MnP

Cited by 36 publications

References 28 publications

Decolorization of different azo dyes by Phanerochaete chrysosporium RP78 under optimal condition

Decolorization of different azo dyes by Phanerochaete chrysosporium RP78 under optimal condition

Optimization of lignin peroxidase production and stability by Phanerochaete chrysosporium using sewage-treatment-plant sludge as substrate in a stirred-tank bioreactor

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

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