Extracellular Peroxidase Enzyme Production in Native Bacteria Bacillus tequilensis and Determination of Some Biochemical Properties of Enzyme

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AHMADI F.; ABBASI A.R.; YAKHCHALI B.; ALIZADE H.; POURBABAEE A.A.

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Journal: JOURNAL OF BIOTECHNOLOGY Year:2020 | Volume:11 | Issue:1 Page(s): 45-52

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Title

Extracellular Peroxidase Enzyme Production in Native Bacteria Bacillus tequilensis and Determination of Some Biochemical Properties of Enzyme

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Keywords

Bacillus tequilensisQ1

PeroxidaseQ2

ThermoalkalophilicQ1

Kinetic ParametersQ1

Abstract

Aims: Peroxidases are used in a wide range of biotechnological applications, most of which are carried out at high temperatures and pHs. Since most of the common Peroxidases in alkaline conditions are unstable and inactive, it is necessary to find Thermoalkalophilic Peroxidases for practical purposes. Materials & Methods: In the present study, the extracellular production of Peroxidase enzyme in the native strain Bacillus tequilensis was studied. For this purpose, the bacteria were cultured in liquid LB medium. Enzyme activity was measured using two substrates 2, 4-DCP and pyrogallol. The effect of culture time on enzyme production as well as the effect of pH and temperature parameters on enzyme activity were investigated. Partial purification of the enzyme was performed by ion exchange chromatography with Sephadex DEAE A50 and the enzyme obtained from the puri􀏐 ication process was used to measure the Kinetic Parameters. Kinetic Parameters such as Km and Vmax were also calculated in this study. Findings: The highest production of Peroxidase enzyme was obtained on the fourth day of bacterial culture. The effect of temperature on the enzyme activity showed the highest amount of enzyme activity at 70° C and the optimum pH of Peroxidase activity was obtained 8 and 10 by using 2, 4-DCP and pyrogallol respectively as substrates. The speci􀏐 ic activity of the enzyme obtained 0. 431 and 0. 833U/ml respectively for the crude enzyme and sample puri􀏐 ied with Sephadex A50, indicating an increase in purity up to approximately two fold after puri􀏐 ication. The enzymes Km and Vmax for pyrogallol were 0. 15mM and 2501. 1U/ml, respectively, and for 2, 4-DCP were 0. 77mM and 0. 97U/ml, respectively. The results of Kinetic Parameters showed that the specificity of this enzyme for pyrogallol is higher. Conclusion: The Peroxidase enzyme produced in the native Bacillus bacterium has the optimum activity at high temperature and pH and since most of the industrial processes are performed under the above conditions, therefore, this enzyme can potentially be used in these processes.

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APA: Copy

AHMADI, F., ABBASI, A.R., YAKHCHALI, B., ALIZADE, H., & POURBABAEE, A.A.. (2020). Extracellular Peroxidase Enzyme Production in Native Bacteria Bacillus tequilensis and Determination of Some Biochemical Properties of Enzyme. JOURNAL OF BIOTECHNOLOGY, 11(1 ), 45-52. SID. https://sid.ir/paper/231182/en

Vancouver: Copy

AHMADI F., ABBASI A.R., YAKHCHALI B., ALIZADE H., POURBABAEE A.A.. Extracellular Peroxidase Enzyme Production in Native Bacteria Bacillus tequilensis and Determination of Some Biochemical Properties of Enzyme. JOURNAL OF BIOTECHNOLOGY[Internet]. 2020;11(1 ):45-52. Available from: https://sid.ir/paper/231182/en

IEEE: Copy

F. AHMADI, A.R. ABBASI, B. YAKHCHALI, H. ALIZADE, and A.A. POURBABAEE, “Extracellular Peroxidase Enzyme Production in Native Bacteria Bacillus tequilensis and Determination of Some Biochemical Properties of Enzyme,” JOURNAL OF BIOTECHNOLOGY, vol. 11, no. 1 , pp. 45–52, 2020, [Online]. Available: https://sid.ir/paper/231182/en

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