pH effect on α-Amylase from porcine pancreas

The Role of Amylase Enzyme in Carbohydrate Hydrolysis

The enzyme amylase catalyzes the mechanism of hydrolyzing starch into simpler and smaller carbohydrate molecules, such as maltose into glucose (Butterworth, Warren & Ellis, 2011).

Types of Amylase Enzyme

According to Whitcomb and Lowe (2007), the enzyme amylase is divided into three types: -Amylase, -Amylase, and -Amylase. Each type of amylase enzyme is special in its activity since they perform best at various pH levels. Whereas -Amylase works better at a pH of 6.7-7.0, -Amylase works best at a pH of 4.0-5.0. -Amylase, on the other hand, performs well under acidic environments since it is active at pH levels of about 3 (Nielsen, Borchert & Vriend, 2001).

The Role of α-Amylase

According to de Almeida, Gregio, Machado, De Lima & Azevedo (2008), α-Amylase helps in breaking down long chain carbohydrates such as amylose into maltose. α-Amylase is mostly found in living organisms where the enzyme plays an active role in the digestion processes, especially in animals. α-Amylase is strategically produced in the digestive systems of most mammals, including human beings, whereby ptyalin enzyme is produced by the salivary glands and the pancreatic amylase by the pancreas. Ptyalin, which is produced in the mouth, when under optimal conditions, Whitcomb & Lowe (2007) observes that it helps break a significant percentage of starch into maltose. On the other hand, pancreatic amylase serves to further catalyze starch not broken down by ptyalin.

Optimal pH for Enzyme Activity

Enzymes work optimally under different pH. While Ptyalin, which is secreted by the salivary gland, has an optimal pH of 4.6 - 5.2, pancreatic amylase from the porcine pancreas works optimally at a pH of 6.7-7.0 (Koukiekolo, Desseaux, Moreau, Marchis-Mouren & Santimone, 2001). According to Nielsen, Borchert & Vriend (2001), the pH factor is a great determiner of how enzymes work. The pH factor has the ability to speed up or lower the rate of functioning of an enzyme or further denature it, making the enzyme non-functioning. Therefore, for pancreatic amylase to work optimally, its pH has to be between 6.7-7.0.

References

Butterworth, P. J., Warren, F. J., & Ellis, P. R. (2011). Human α‐amylase and starch digestion: An interesting marriage. Starch‐Stärke, 63(7), 395-405.

de Almeida, P. D. V., Gregio, A. M., Machado, M. A., De Lima, A. A., & Azevedo, L. R. (2008). Saliva composition and functions: a comprehensive review. J Contemp Dent Pract, 9(3), 72-80.

Koukiekolo, R., Desseaux, V., Moreau, Y., Marchis‐Mouren, G., & Santimone, M. (2001). Mechanism of porcine pancreatic α‐amylase. European journal of biochemistry, 268(3), 841-848

Nielsen, J. E., Borchert, T. V., & Vriend, G. (2001). The determinants of α-amylase pH–activity profiles. Protein engineering, 14(7), 505-512.

Whitcomb, D. C., & Lowe, M. E. (2007). Human pancreatic digestive enzymes. Digestive diseases and sciences, 52(1), 1-17.