Alberte, J., Pitzer, T. Calero, K. Enzymes. In: General Biology I Lab Manual. (2012). 2nd edition. p. 49, New York, NY: Mc Graw Hill Education.
The lab manual describes how enzymes significantly improve our standard of living. Just like our own body creates enzymes such as Proteases as well as Amylases to break down starches and proteins, enzymes are also used commercially to bake bread, biscuits, and crackers. Enzymes are also used in the making of alcohol, cheese, as well as detergents. In the field of medicine, enzymes are very important in the treatment of heart attacks and cancer.
Horowitz, Benjamin. (1918). What are enzymes. In: The Scientific Monthly, Vol. 6. n.p, pp. 253- 259. New York: Columbia University.
Horowitz explains the basics of what enzymes and what catalysts are. The word Enzyme comes from the Greek word meaning yeast. The most acceptable definition even with today’s scientific advances is to call it a substance which shows the properties of a catalyst and is the produced as a result of cellular activity. Horowitz continues to explain what a catalyst is. His definition, a rather simple one, is a substance that accelerates a reaction. The enzyme is like a lock and key to the specific substrate that it will be attaching to. In the yeast cell for example, you can find the degree of specificity. The yeast cell has sucrase, which can only act on sucrose. If you were to attempt to break down sucrose with any other enzyme it simply wouldn’t work.
Bajpai, P., Bajpai, P. K. (2004, February 18). High‐temperature alkaline α‐amylase from Bacillus Licheniformis TCRDC‐B13. In: Biotechnology and Bioengineering, Vol. 33, pp. 72-78
This experiment tested for the optimal conditions of Bacillus Licheniformis. Conditions s such as types of carbon and nitrogen sources, temperature, pH, and time of reaction for production of α‐amylase were tested. In Pramod and Pratima’s experiment, the enzyme showed optimal activity at around 90˚C, however, it was also active at 100˚C. The Bacillus Licheniformis presented optimum activity in the broad pH range 5.5–10.
Suman, S., & Ramesh, K. (2010). Production of a thermostable extracellular amylase from thermophilic Bacillus species. In: Journal of Pharmaceutical Sciences and Research, Vol. 2, pp. 149–154.
Amylases are one of the most important enzymes in present day biotechnology. The
reason for this being the wide range of its’ potential application. The practical application of Amylase has come a long way since its first use as a pharmaceutical aid in the treatment of digestive disorders in 1894. In the world of industrial enzymes, Amylases constitute twenty-five percent of the enzyme market. Amylases have the potential application in many industrial processes. Some of these include the production of food, the making of bread, the production of alcoholic beverages. Amylases are also responsible for sweeteners such as glucose and fructose syrups as well as fruit juices.
Smith, A. M., Zeeman, S. C., & Smith, S. M. (2005). Starch degradation. In: Annu Rev Plant Biol, Vol. 56, pp. 73-98
The physical breakdown of starch is explained in this source. Starch in chloroplast is in the form of granules composed of branched polymers of glucose. The first step in the pathway of starch degradation must therefore be catalyzed by an enzyme capable of metabolizing polymers at the surface of a granule, rather than in a soluble form. Although several different types of enzymes are capable of releasing soluble glucans from purified starch granules, the only enzyme generally believed to do this in plant is amylase.
Urry, L. A., Cain, M. L., Wasserman, S. A., Minorsky, P. V., Reece, J. B., & Campbell, N. A. (2016). Campbell Biology in Focus. Harlow: Pearson Education Limited.
