Purification and some properties of Mn peroxidase from Lentinula edodes

Bôer, Cinthia Gandolfi; Obici, Larissa; Souza, Cristina Giatti Marques de; Peralta, Rosane Marina

doi:10.1016/j.procbio.2005.11.025

Cited by 51 publications

(39 citation statements)

References 24 publications

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“…F17 which exhibited 89% relative activity in the presence of 1 mM Ca 2+ . In another study, Ca 2+ had insignificant effect on POX activity [41]. Similar to our results on activation of total POX from A. viscosus by Ca 2+ is the report by Praveen et al [37] on POX from Stereum ostrea.…”

Section: Effect Of Edta and Metal Ions On Activity Of Total Poxssupporting

confidence: 92%

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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Section: Effect Of Edta and Metal Ions On Activity Of Total Poxssupporting

confidence: 92%

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

Olajuyigbe¹,

Ehiosun²,

Jaiyesimi³

2015

AER

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“…melanoidins) is largely depend on the medium pH as it is less soluble in acidic than in alkaline pH (Mohana et al 2007). It was also observed that increase in temperature from 30 to 37°C was accompanied with increased degradation of color containing compounds and further, increase in temperature ([37°C) adversely affected the degradation of color containing compounds possibly due to the loss of enzyme activity at higher temperature (Boer et al 2006).…”

Section: Resultsmentioning

confidence: 99%

Biodegradation of the major color containing compounds in distillery wastewater by an aerobic bacterial culture and characterization of their metabolites

Bharagava

Chandra

2010

Biodegradation

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This study deals the biodegradation of the major color containing compounds extracted from distillery wastewater (DWW) by an aerobic bacterial consortium comprising Bacillus licheniformis (DQ79010), Bacillus sp. (DQ779011) and Alcaligenes sp. (DQ779012) and characterization of metabolic products. The degradation of color containing compounds by bacteria was studied by using the different carbon and nitrogen sources at different environmental conditions. Results revealed that the bacterial consortium was efficient for 70% color removal in presence of glucose (1.0%) and peptone (0.1%) at pH 7.0 and temperature 37 degrees C. The HPLC analysis of control and bacterial degraded samples has shown the reduction in peak area as well as shifting of peaks compared to control indicating the bacterial degradation as well as transformation of color containing compounds from DWW. The comparative LC-MS-MS and other spectrophotometric analysis has shown the presence of dihydroxyconiferyl alcohol, 2, 2'-bifuran-5-carboxylic acid, 2-nitroacetophenone, p-chloroanisol, 2, 3-dimethyl-pyrazine, 2-methylhexane, methylbenzene, 2, 3-dihydro-5-methylfuran, 3-pyrroline, and acetic acid in control samples that were biodegraded and biotransformed into 2-nitroacetophenone, p-chloroanisol, 2, 2'-bifuran, indole, 2-methylhexane, and 2, 3-dihydro-5-methylfuran by bacterial consortium. In this study, it was observed that most of the compounds detected in control samples were diminished from the bacterial degraded samples and compounds 2, 2'-bifuran and indole with molecular weight 134 and 117 were produced as new metabolites during the bacterial degradation of color containing compounds from DWW.

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“…The crude extract was submitted to protein concentration for acetone precipitation at a ratio of 1:3 (v/v -crude extract: acetone) according to a method proposed by Boer et al, 12 adapted for this work. The mixture was allowed to rest in refrigeration for 24 h. Then it was centrifuged at 5000 rpm at 4 °C for 40 min, and the precipitate was subsequently solubilized in 5 mmol L -1 phosphate buffer pH 5.…”

Section: Exclusion Molecular Chromatographymentioning

confidence: 99%

Peroxidase from soybean meal: obtention, purification and application in reduction of deoxynivalenol levels

Feltrin¹,

Fontes²,

Gracia³

et al. 2017

Quim. Nova

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This study established the conditions for the extraction of the enzyme peroxidase (PO) from soybean meal (SBM). An experimental design methodology was carried out in order to evaluate the effects of stirring rate time, pH and extracting solvent volume on the enzyme extraction. By using 5 g SBM and 50 mL phosphate buffer 10 mmol L -1 pH 4.7, 60 min stirring rate at 100 rpm, an enzyme with specific activity of 100 U mg -1 for SBM was obtained. Two techniques of purification were tested and compared for purification of peroxidase from soybean meal: triphasic partition (TPP) and molecular exclusion chromatography. TPP showcased a greater efficiency with 50% recuperation and a purification factor of 13.6. Peroxidase in crude and pure forms was characterized for kinetics, thermodynamics and biochemistry. The parameter of thermal inactivation indicates high stability to exposure time and temperature increase, showing that enzyme activity is not altered by the presence of constituents of the reaction medium. Peroxidase in crude form represented a greater upkeep in activity, keeping 50% activity for 114 days at 0 °C. Peroxidase in pure form had greater affinity for substrate and reduced Deoxynivalenol levels by 80%, 20% more than the crude form.

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Purification and some properties of Mn peroxidase from Lentinula edodes

Cited by 51 publications

References 24 publications

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

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

Biodegradation of the major color containing compounds in distillery wastewater by an aerobic bacterial culture and characterization of their metabolites

Peroxidase from soybean meal: obtention, purification and application in reduction of deoxynivalenol levels

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