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Biobleaching of industrial important dyes with peroxidase partially purified from garlic.

Osuji AC, Eze SO, Osayi EE, Chilaka FC - ScientificWorldJournal (2014)

Bottom Line: The Km and V max for H2O2 and o-dianisidine were 0.026 mM and 0.8 U/min, and 25 mM and 0.75 U/min, respectively.Peroxidase from garlic was effective in decolourizing Vat Yellow 2, Vat Orange 11, and Vat Black 27 better than Vat Green 9 dye.For all the parameters monitored, the decolourization was more effective at a pH range, temperature, H2O2 concentration, and enzyme concentration of 4.5-5.0, 50°C, 0.6 mM, and 0.20 U/mL, respectively.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, University of Nigeria, Nsukka, Nigeria.

ABSTRACT
An acidic peroxidase was extracted from garlic (Allium sativum) and was partially purified threefold by ammonium sulphate precipitation, dialysis, and gel filtration chromatography using sephadex G-200. The specific activity of the enzyme increased from 4.89 U/mg after ammonium sulphate precipitation to 25.26 U/mg after gel filtration chromatography. The optimum temperature and pH of the enzyme were 50°C and 5.0, respectively. The Km and V max for H2O2 and o-dianisidine were 0.026 mM and 0.8 U/min, and 25 mM and 0.75 U/min, respectively. Peroxidase from garlic was effective in decolourizing Vat Yellow 2, Vat Orange 11, and Vat Black 27 better than Vat Green 9 dye. For all the parameters monitored, the decolourization was more effective at a pH range, temperature, H2O2 concentration, and enzyme concentration of 4.5-5.0, 50°C, 0.6 mM, and 0.20 U/mL, respectively. The observed properties of the enzyme together with its low cost of extraction (from local sources) show the potential of this enzyme for practical application in industrial wastewater treatment especially with hydrogen peroxide. These Vat dyes also exhibited potentials of acting as peroxidase inhibitors at alkaline pH range.

Show MeSH
Effect of temperature on peroxidase activity.
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fig4: Effect of temperature on peroxidase activity.

Mentions: Figure 4 shows an optimum temperature of 50°C for the enzyme. When the temperature exceeds 50°C, the activity began to decline. Haq et al. [20] recorded an optimum activity at 55°C for peroxidase from Raphanus sativus. Onder et al. [23] reported an optimum temperature of 30°C for peroxidase from Turkish black radish using guiacol as substrate. Mamounata et al. [24] recorded an optimum temperature range of 30–40°C for peroxidases from Raphanus sativus, Allium sativum, Ipomoea batatas, and Sorghum bicolor grown in Burkina Faso. Matto and Husain [25] observed an optimum temperature of 50°C for cabbage peroxidase and 40°C for radish and tobacco peroxidases. The result of this study is also comparable with the optimum temperature reported by Omidiji et al.[26] for peroxidase from Dioscorea esculenta L. tubers. The enzyme was found to be less thermostable at higher temperatures (Figure 5). It was found to be thermostable at 40, 50, and 60°C, respectively. The thermostability dropped drastically at 70 and 80°C within 10 min of heat treatment (Figure 5) suggesting that high temperature short time treatment could easily inactivate the enzyme.


Biobleaching of industrial important dyes with peroxidase partially purified from garlic.

Osuji AC, Eze SO, Osayi EE, Chilaka FC - ScientificWorldJournal (2014)

Effect of temperature on peroxidase activity.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4226186&req=5

fig4: Effect of temperature on peroxidase activity.
Mentions: Figure 4 shows an optimum temperature of 50°C for the enzyme. When the temperature exceeds 50°C, the activity began to decline. Haq et al. [20] recorded an optimum activity at 55°C for peroxidase from Raphanus sativus. Onder et al. [23] reported an optimum temperature of 30°C for peroxidase from Turkish black radish using guiacol as substrate. Mamounata et al. [24] recorded an optimum temperature range of 30–40°C for peroxidases from Raphanus sativus, Allium sativum, Ipomoea batatas, and Sorghum bicolor grown in Burkina Faso. Matto and Husain [25] observed an optimum temperature of 50°C for cabbage peroxidase and 40°C for radish and tobacco peroxidases. The result of this study is also comparable with the optimum temperature reported by Omidiji et al.[26] for peroxidase from Dioscorea esculenta L. tubers. The enzyme was found to be less thermostable at higher temperatures (Figure 5). It was found to be thermostable at 40, 50, and 60°C, respectively. The thermostability dropped drastically at 70 and 80°C within 10 min of heat treatment (Figure 5) suggesting that high temperature short time treatment could easily inactivate the enzyme.

Bottom Line: The Km and V max for H2O2 and o-dianisidine were 0.026 mM and 0.8 U/min, and 25 mM and 0.75 U/min, respectively.Peroxidase from garlic was effective in decolourizing Vat Yellow 2, Vat Orange 11, and Vat Black 27 better than Vat Green 9 dye.For all the parameters monitored, the decolourization was more effective at a pH range, temperature, H2O2 concentration, and enzyme concentration of 4.5-5.0, 50°C, 0.6 mM, and 0.20 U/mL, respectively.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, University of Nigeria, Nsukka, Nigeria.

ABSTRACT
An acidic peroxidase was extracted from garlic (Allium sativum) and was partially purified threefold by ammonium sulphate precipitation, dialysis, and gel filtration chromatography using sephadex G-200. The specific activity of the enzyme increased from 4.89 U/mg after ammonium sulphate precipitation to 25.26 U/mg after gel filtration chromatography. The optimum temperature and pH of the enzyme were 50°C and 5.0, respectively. The Km and V max for H2O2 and o-dianisidine were 0.026 mM and 0.8 U/min, and 25 mM and 0.75 U/min, respectively. Peroxidase from garlic was effective in decolourizing Vat Yellow 2, Vat Orange 11, and Vat Black 27 better than Vat Green 9 dye. For all the parameters monitored, the decolourization was more effective at a pH range, temperature, H2O2 concentration, and enzyme concentration of 4.5-5.0, 50°C, 0.6 mM, and 0.20 U/mL, respectively. The observed properties of the enzyme together with its low cost of extraction (from local sources) show the potential of this enzyme for practical application in industrial wastewater treatment especially with hydrogen peroxide. These Vat dyes also exhibited potentials of acting as peroxidase inhibitors at alkaline pH range.

Show MeSH