Inhibitory studies of peroxidase from infected African eggplant (&lt;i&gt;Solanum aethiopicum&lt;/i&gt;) fruit

Omeje, Kingsley O.; Ezema, Benjamin E.; Ozioko, J.N.; Eze, Sabinus Oscar Onyebuchi; Chilaka, Ferdinand Chiemeka

doi:10.4314/jasem.v23i11.7

Cited by 2 publications

(7 citation statements)

References 6 publications

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“…The specific activity of the crude enzyme was 13.90 U/mg, which increased to 35.80 U/mg and 55.46U/mg after (NH4)2SO4 precipitation and gel filtration respectively. This result corroborate the report by Omeje et al (2019), who stated that for purification procedure to be successful, the specific activity of the desired enzyme must be greater than the former after each purification step. Peroxidase extracted from oil palm (Elaeis guineensis) leaves was purified four folds in this study.…”

Section: Resultssupporting

confidence: 91%

Studies on the Thermal Stability of Peroxidase from Leaf of Oil Palm (Elaeis guineensis)

Ozioko¹,

Ezema²,

Omeje³

et al. 2021

jasem

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Peroxidase was extracted from leaves of oil palm tree with 0.01M phosphate buffer pH 7.0. It was partially purified using 70% ammonium sulphate ((NH4)2SO4) precipitation. This resulted in peroxidase with activity of (26U/ml) and specific activity of 35.8U/mg. Effect of heat on the activity of peroxidase was studied at temperature of 323-363°K. After gel filtration on sephadex G100, the peroxidase activity increased to 27U/ml, with specific activity of 55U/mg .The overall purification fold was 4 with 51.9% enzyme recovery. The peroxidase partially purified from leaves of oil palm tree showed pH and temperature optima of 5.0 and 50°C respectively. High pH and temperature stabilities of pH 5.0 to pH 9.0 and 50°C to 70°C were obtained respectively. Also, the activation energy (Ea) of the reaction was - 21.616kj/mol. The free energy changes (ΔG) were 96008.64, 96315.59, 97901.63, 94132.33 and 97146.75kj/mol at 323,333,343,353 and 363°K respectively. It was observed that the D-values were decreasing with increasing temperature with a Z-value of 0.044. The enthalpy results suggest that the reaction was exothermic, non-spontaneous and reversible.

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Section: Resultssupporting

confidence: 91%

Studies on the Thermal Stability of Peroxidase from Leaf of Oil Palm (Elaeis guineensis)

Ozioko¹,

Ezema²,

Omeje³

et al. 2021

jasem

Self Cite

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“…Then excess ammonium sulfate was removed through dialysis. Enzyme activity increased to 304.52 U/mg [11].…”

Section: Partial Purification and Extraction Of Peroxidasementioning

confidence: 94%

“…Peroxidase activity is evaluated calorimetrically using a spectrophotometer (Cecil 7200) following tetraguaiacol formation at λ max = 470 nm. The quantity of enzyme that catalyzes 1 mol of guaiacol in 1 min is defined as one unit of peroxidase activity [11]. The optimum pH for peroxidase activity was achieved by measuring the enzyme's activity using buffers in the pH range of 2-10: glycine HCL (pH 2-4), acetate (pH 5-6), phosphate (pH 7-8) and tris-HCl (pH 9-10) [9].…”

Section: Enzyme Characterization and Assaymentioning

confidence: 99%

“…For optimal pH, the behavior of Citrus limon peroxidase (CLP) was shown through graph Fig. 1a utilizing pH buffers raging (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12). At pH 5, CLP activity was observed at its peak.…”

Section: Ph Effect and Ph Stabilitymentioning

confidence: 99%

“…[10]. Peroxidases are thermally stable, highly effective in milder reaction conditions, and catalytically non-selective [11]. Peroxidases are associated with various physiological processes, including tissue healing and cross-connection of polysaccharide cell walls, tissue repair, pathogen resistance mechanisms, chloroplast and cytosol scavenging of H 2 O 2 , heavy metals detoxification, and reactive oxygen species during oxidative stress and cellular metabolic procedure, and biodegradation reactions.…”

Section: Introductionmentioning

confidence: 99%

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Citrus limon peroxidase-assisted biocatalytic approach for biodegradation of reactive 1847 colfax blue P3R and 621 colfax blue R dyes

Riaz

Kalsoom

Bhatti

et al. 2022

Bioprocess Biosyst Eng

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One of the big environmental problems in today’s world is dye-contaminated toxic waste. Peroxidase is known as highly efficient for the degradation of various pollutants, including dyes. Environmental contamination caused by the discharge of dyes into water bodies is an onerous challenge that poses both human and ecological hazards. In the current studies, biocatalysts used for enzyme decolorization (1847 Colafx Blue P3R and 621 Colafx Blue) are regarded as an eco-friendly method utilizing commonly available low-cost material lemon peels (Citruslimon peroxidase). Peroxidase was extracted in a phosphate buffer of pH 7.0 and partially purified by 20–80% ammonium sulfate precipitation technique from Citruslimon peels. The soluble enzyme was characterized in terms of kinetic and thermodynamic parameters. The values of Km and Vmax (23.16 and 204.08 μmol/ml/min) were determined, respectively. The enzyme showed maximum activity at pH 5.0 and a temperature of 55 °C. Citruslimon efficiently degraded 1847 Colafx Blue P3R and 621 Colafx Blue R dyes with maximum degradation of 83 and 99%, respectively, with an initial dye concentration of 200 ppm at pH 4 and 35 °C temperature within 5–10 min of incubation time. The effect of the redox mediator on the degradation process was examined. Results showed that the peroxidase HOBT system efficiently enhanced the degradation of dyes from water. Hence, Citruslimon peroxidase is an efficient biocatalyst for the treatment of effluents.

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Inhibitory studies of peroxidase from infected African eggplant (<i>Solanum aethiopicum</i>) fruit

Cited by 2 publications

References 6 publications

Studies on the Thermal Stability of Peroxidase from Leaf of Oil Palm (Elaeis guineensis)

Studies on the Thermal Stability of Peroxidase from Leaf of Oil Palm (Elaeis guineensis)

Citrus limon peroxidase-assisted biocatalytic approach for biodegradation of reactive 1847 colfax blue P3R and 621 colfax blue R dyes

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