Extraction and partial purification of urease enzyme from Jack fruit

Simon Chouhan (1) , Vishnu Priya V (2) , Gayathri R (3)
(1) Department of Biochemistry, Saveetha Dental College, Saveetha Institute of Medical and Technical Sciences, Saveetha University, Velappanchavadi, Chennai - 600077, Tamil Nadu, India, India ,
(2) Department of Biochemistry, Saveetha Dental College, Saveetha Institute of Medical and Technical Sciences, Saveetha University, Velappanchavadi, Chennai - 600077, Tamil Nadu, India, India ,
(3) Department of Biochemistry, Saveetha Dental College, Saveetha Institute of Medical and Technical Sciences, Saveetha University, Velappanchavadi, Chennai - 600077, Tamil Nadu, India, India

Abstract

Jackfruit (Artrocarpus Heterophyllus) has a place with family Moraceae is a basic piece of normal Indian eating routine. Urease, one of the very productive known catalysts catalyzes the hydrolysis of urea into NH3 and carbon dioxide. The present study aimed to extract urease enzyme from jackfruit. The protein extraction was done from jackfruit, after dialysis and precipitation, isolated urease was characterised by determining optimum pH and temperature and finally confirmed by the protein isolation technique, SDS-PAGE gel electrophoresis. The optimum temperature of urease activity was found to be 40 degree Celsius. The optimum pH of urease activity was found to be 6.9. The molecular weight of partially purified urease is 90 KDa. Thus, urease enzyme isolated from jackfruit source showed potential activity on physiological functions in human beings. Since plant urease enzyme is used as a vaccine. In future; the study can be extended in purifying the enzyme and it can be used for clinical aspects.

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Authors

Simon Chouhan
Vishnu Priya V
drvishnupriyav@gmail.com (Primary Contact)
Gayathri R
Simon Chouhan, Vishnu Priya V, & Gayathri R. (2018). Extraction and partial purification of urease enzyme from Jack fruit. International Journal of Research in Pharmaceutical Sciences, 9(2), 438–441. Retrieved from https://ijrps.com/home/article/view/4231

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