The Effect of Temperature on Enzymatic Activity of Amylase - Lab Report Example

Download file to see previous pages The rate of reaction was directly proportional to the increase in temperature, but there was a decline after 40°C as envisaged in the hypothesis, the enzymes denature with a very high elevation in temperature, concluding that if the temperature is increased beyond the optimal temperature then the enzymatic activities come to a close and enzyme becomes denatured. The study also envisaged that fungal amylase does display the slightly faster hydrolytic action on starch as compared to the human salivary amylase.

Starch is a regular component of our daily diet. It is perhaps an extensive carbohydrate in the plant world and is consumed by humans and other herbivores to meet their energy requirements. It is a polymer of glucose which depicts the linkage of α-1,4 and α-1,6 glucosidic bonding. It is essential to break this bonding to derive carbon and energy from the starch molecules; this task is performed by a group of enzymes called amylases (Lehninger, 2008).

There are various organisms that serve as sources of amylase, human saliva, and pancreas, other organisms encompass plants fungi and bacteria. The present study includes two groups of amylases, human amylase, and fungal amylase. Human amylase was obtained from the saliva while the fungal amylase was procured from Aspergillus species which is highly prevalent and generally acquired from the soil, putrefying foliage and also present in the air.

Any reaction needs some initiation energy for its onset; this is also true for biological processes. Hydrolysis of starch also requires some activation energy but due to the presence of biological catalysts, enzyme amylase this activation energy can be reduced and the reaction is carried out with ease. Enzymes are extremely specific for substrates, pH, temperature.  ...Download file to see next pagesRead More