Enzyme
Aim
To investigate the effect of different temperatures on the activity of rennin in milk
Introduction
Enzymes are globular protein, responsible for most of the chemical activities of living organisms. They are made up of long chains of amino acids containing carbon, hydrogen, oxygen and nitrogen (Gunsch, 2012). The role of enzyme is to act as catalysts, substances that speed up chemical reactions without being chemically altered during the process. The speeding up of chemical reactions is done by lowering the activation energy required to start a reaction. Enzymes are specific in their actions, and they contain active sites that will temporarily bind to a specific substrate for the bonds in the substrate to be broken and the products to be released. Every enzyme has a set of optimum conditions. Factors like temperature, pH and substrate concentration have an impact on enzyme activity.
In this experiment, the enzyme Rennin, a type of proteolytic enzyme that is usually used to coagulate milk to make cheese, was used. Rennin usually serve as protein-digesting enzyme that coagulates milk by transforming soluble caseinogen into insoluble casein in the form of curd like structure (Whitaker, n.d). Rennin can be found in the gastric juice of cud-chewing animal such as cow (Whitaker, n.d). Rennin like every enzyme has a certain temperature range where it can function most efficiently. For rennin, the optimum temperature is around 37 oC – 40 oC in correspondence with the internal mammalian body temperature.
The objective of this experiment was to determine the effects of different temperature conditions on the activity and functionality of the enzyme in the enzyme-catalysed reaction. It is expected that the rate of reaction will increase as the temperature increases until it reaches the optimal temperature of 37 oC – 40 oC, then abruptly decline with further increase of temperature. Beyond the optimal temperature, the rate of reaction will begin to slow down and
To investigate the effect of different temperatures on the activity of rennin in milk
Introduction
Enzymes are globular protein, responsible for most of the chemical activities of living organisms. They are made up of long chains of amino acids containing carbon, hydrogen, oxygen and nitrogen (Gunsch, 2012). The role of enzyme is to act as catalysts, substances that speed up chemical reactions without being chemically altered during the process. The speeding up of chemical reactions is done by lowering the activation energy required to start a reaction. Enzymes are specific in their actions, and they contain active sites that will temporarily bind to a specific substrate for the bonds in the substrate to be broken and the products to be released. Every enzyme has a set of optimum conditions. Factors like temperature, pH and substrate concentration have an impact on enzyme activity.
In this experiment, the enzyme Rennin, a type of proteolytic enzyme that is usually used to coagulate milk to make cheese, was used. Rennin usually serve as protein-digesting enzyme that coagulates milk by transforming soluble caseinogen into insoluble casein in the form of curd like structure (Whitaker, n.d). Rennin can be found in the gastric juice of cud-chewing animal such as cow (Whitaker, n.d). Rennin like every enzyme has a certain temperature range where it can function most efficiently. For rennin, the optimum temperature is around 37 oC – 40 oC in correspondence with the internal mammalian body temperature.
The objective of this experiment was to determine the effects of different temperature conditions on the activity and functionality of the enzyme in the enzyme-catalysed reaction. It is expected that the rate of reaction will increase as the temperature increases until it reaches the optimal temperature of 37 oC – 40 oC, then abruptly decline with further increase of temperature. Beyond the optimal temperature, the rate of reaction will begin to slow down and
References: Allogio, V, Caponio, F, Pasqualone A & Gomes, T 2000, ‘Effect of heat treatment on the rennet clotting time of goat and cow milk’, Journal of Food Chemistry, vol.70, no.1, pp.51-55, viewed on 26 May 2013, from . Barker, JR, (n.d), ‘Temperature and Enzyme Activity’, Department of Zoologogy and Comparative Anatomy, Oxford, pp.723-727, viewed on 29 May 2013, from Bowen, R, 1996, Chymosin (Rennin) and the Coagulation of Milk, accessed 28 May 2013 from . Gunsch, J, 2012, What are enzymes, viewed on 28 May 2013, from . John, D (2012), Effect of Temperature on Enzyme Activity, viewed on 29 May 2013, from Whitaker, E, (n.d.),The Effect of Temperature on the Enzyme Rennin, accessed on 28 May 2012 from .