Extraction and Purification of Fruit Bromelain

Presenter: Sonia Gonzalez

Co-Presenter(s):
Natalie Asemi

Presenter Status: Undergraduate student

Department: Chemistry

Screenshot URL: https://drive.google.com/uc?id=1ObCqt6hRSon9BXFOJ0ybh6zcy3CoVLvm

Abstract:
The pineapple plant (Ananas comosus) contains at least four distinct sulfhydryl proteolytic enzymes. Fruit and stem bromelain have been identified as the major protease of A. Comosus with ananain. The proteolytic fraction of pineapple stem is termed stem bromelain, while the one present in the fruit is known as fruit bromelain. The amino acid sequence and domain analysis of the fruit and stem bromelain demonstrate several difference and similarities of these cysteine protease family members. Fruit bromelain (EC 3.4.22.33) has a molecular weight of 31 kDa, an isoelectric point, pH 4.6, and absorbance at 280 nm. In our investigation, commercial bromelain was assayed for its activity by casein digestion method, represented by using casein digestion unit. Our standard curve showed that as the enzyme concentration increased, so did its activity with the slope to be found at .0024. Moreover, these methods demonstrate ways in which one can assess the proteolytic activity of fruit bromelain.