Introduction

An enzyme is a biological catalyst within living organisms. It controls the rate at which chemical reactions occur without altering its natural structure or chemistry during the entire process. Chemical reactions facilitate normal functioning of the body. Either without the presence of enzymes, some of the reactions would fail to take place or they would occur at a slower rate than usual. Temperature, ph., and the concentration of substrate affect enzyme activities. The substrate binds onto the active site of an enzyme during chemical reaction processes (Bisswanger & Wiley, 2017).

The experiment focuses on substrate casein, found in milk and enzyme rennin or chymosin. Chymosin is an enzyme found in the stomach of various animals. Chymosin coagulates milk in the stomach of animals. Without coagulation of milk, digestion of protein milk would not take place. Chymosin converts milk into a semisolid substance consequently increases its chances of storage in the stomach. According to the experiment, the substrate is the dependent variable and the enzyme is the independent variable (Bisswanger & Wiley, 2017).

Hypothesis and reasoning

If the substrate concentration increases, then the chemical reaction between rennin and substrate Casein increases. However, the number of active sites remains limited. During the chemical reaction, all the enzyme’s active sites combine with the substrate, in this case casein, which in turn increases the reaction. More so, the maximum reaction occurs when the substrate occupy all the active sites until the saturation point. The reaction levels off at a certain point. The presence of a high number of substrate indicates saturation of enzymes within the chemical reaction (Bisswanger & Wiley, 2017).

Procedure

 A reaction between enzyme rennin and substrate casein in the laboratory. The observations that take place between in enzyme rennin in milk and casein are subject of discussion. First, the activity of rennin is hydrolytic in nature hence splits casein into particles of paracasein. Secondly, after the split of casein would make it easier for coagulation to take place (Buchholz, Kasche, & Bornscheuer, 2012).

During experiment, when preparing casein solutions, mixing pure casein and lime, and then shaking vigorously. Another way is grinding calcium carbonate instead of using lime liquid. Therefore, the casein solutions are neutral in nature and to litmus. The curds from the reaction sieved off and the remaining solution checked for races of nitrogen. Nitrogen solution was present but it was not constant and did not have any links to rennin and casein utilized during the experiment (Buchholz, Kasche, & Bornscheuer, 2012).

In the control side of the experiment, addition of enzyme rennin into the casein solution did not take place. However, nitrogen found in both the control and the actual experiment was similar. In the control experiment, filtering out of the nitrogen was not possible. Besides, nitrogen, acetic acid was present. Casein solutions prepared for the experiment contain basic components of caseinates, which may either basic or neutral. Casein solutions can undergo auto hydrolysis, which can explain the presence of nitrogen during the experiment (Buchholz, Kasche, & Bornscheuer, 2012).

Results

A mixture of flask with 150cc of pure water, 75 cc lime liquid, and tuol. Shaking the content of the flask saturated it with casein and in turn, the resulting mixture was calcium caseinate, which was basic in nature. The separation of undissolved casein from the solution through centrifuging and sieving to determine the amount of casein in solution alone. The solution had 50cc. Portion of the 50cc were drawn at various intervals and precipitated with acetic acid (Buchholz, Kasche, & Bornscheuer, 2012).

Discussion of the results

In order to understand the action of rennin one needs to know the specific roles of the enzymes plays. Rennin curdles milk in the stomach of animals like goat and a lamb. Curdling milk converts it into a semisolid substance such as a cheese. The resulting semi solid substance is durable within the stomach. The production of rennin is highest during the first days after birth. Amount reduces as time goes by and pepsin replaces the enzyme. Rennin occurs in an inactive form known as prochymosin. Later an acid activates the enzyme and helps it perform its functions (Stubbs, Suleyman, & Horton-Szar, 2014).

 The aim of the experiment was to clarify that if substrate concentration increases, the chemical reaction catalyzed by the enzyme increases. High substrate concentration increases the active upon which enzymes can act on. Thus, in the end, increase in substrate increases the pace of the chemical reaction. It is vital to note that the reaction levels of at some point due to enzyme concentration and by products formed that slow down the entire process (Stubbs, Suleyman, & Horton-Szar, 2014).

 Conclusion

A calcium caseinate solution neutral in nature is free from rennin. Another solution of calcium casienate, acidic when submitted to a litmus test and has basic properties is subject to curdling by rennin. Ammonium and potassium caseinates may not experience curdling by rennin. In such solutions, the casein converts into paracasein, which are soluble bases. Formation of a paracasein in the presence of a rennin, allows no other by-product to form. Thus, rennin acts on substrates when within acidic conditions. More so, acidic nature activates the enzyme further. Hence, optimum conditions for rennin must be acidic.

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

References

 

Bisswanger, H., & Wiley-VCH,. (2017). Enzyme Kinetics: Principles and Methods.

Buchholz, K., Kasche, V., & Bornscheuer, U. T. (2012). Biocatalysts and enzyme technology. Weinheim: Wiley.

Stubbs, M., Suleyman, N., & Horton-Szar, D. (2014). Crash Course: Cell Biology and Genetics. Saint Louis: Elsevier Health Sciences UK.