Production and characterisation of peroxidase from Brassica oleracea (Cabbage)

Prerna Jain (1) , Gayathri R (2) , Vishnu Priya V (3)
(1) Department of Biochemistry, Saveetha Dental College, Saveetha Institute of Medical and Technical Science, Saveetha University, Chennai - 600 077, Tamil Nadu, India, India ,
(2) Department of Biochemistry, Saveetha Dental College, Saveetha Institute of Medical and Technical Science, Saveetha University, Chennai - 600 077, Tamil Nadu, India, India ,
(3) Department of Biochemistry, Saveetha Dental College, Saveetha Institute of Medical and Technical Science, Saveetha University, Chennai - 600 077, Tamil Nadu, India, India

Abstract

Peroxidases, are the enzymes which decomposes hydrogen peroxide and also acts as an antioxidant. The plant peroxidases are involved in various biochemical processes and development and also has a role in defence. Brassica oleracea var. capitata (cabbage) being the source of peroxidase have been employed for the remediation of commercial dyes. Pure cabbage extract was prepared by adding buffers, extraction of proteins and protein dialysis was done. The extracted assay and concentrated enzyme was characterized for its optimum pH and temperature. The protein was fractionated using SDS - PAGE electrophoresis to find the approximate molecular weight. Once the research was performed, the optimum pH for peroxidase activity was found to be 6.0 whereas the optimum temperature for peroxidase activity was calculated to be 45°C and the molecular weight of the partially purified peroxidase enzyme is 43kDa. Peroxidase have many possibilities of clinical applications. They can be used as a diagnostic kit for Glucose and in waste water treatment.

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Authors

Prerna Jain
Gayathri R
gayathri.jaisai@gmail.com (Primary Contact)
Vishnu Priya V
Prerna Jain, Gayathri R, & Vishnu Priya V. (2018). Production and characterisation of peroxidase from Brassica oleracea (Cabbage). International Journal of Research in Pharmaceutical Sciences, 9(3), 519–523. Retrieved from https://ijrps.com/home/article/view/4246

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