Biochemical studies of the bromelain enzimatic activity of the enzyme pineapple Ananas comusus
Keywords:
biochemical characterization, plant protease, pineapple, Kunitz, cv PérolaAbstract
This study aimed to determine bromelain enzimatic activity of the enzyme pineapple Ananas comusus cv. Pérola in both in vivo and in natura conditions and partial biochemical characterization of this enzyme that is widely used in pharmaceutical and food industries. The proteolytic activity was measured by digestion of casein by the Kunitz (1947) method. Higher activity was observed for bromelain extracted from pineapple fruits when compared to leaves of pineapple cultured in natura under hydroponic condition. The variation in proteolytic activity due to pH and temperature was determined at pHs between 4.0 to 9.0, and temperatures between 20ºC to 70°C. Bromelain showed optimum pH of action 5.0 in sodium acetate buffer and optimum temperature of 40ºC.Downloads
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França-Santos, A., Alves, R. S., Leite, N. S., & Fernandes, R. P. M. (2011). Biochemical studies of the bromelain enzimatic activity of the enzyme pineapple Ananas comusus. Scientia Plena, 5(11). Retrieved from https://scientiaplena.emnuvens.com.br/sp/article/view/749
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