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Essay about Determining Vmax and Km of Alkaline Phosphatase

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1. Introduction
1.1. Aim
1.2. Theory and principles
1.3. Application of principles
2. Experimental
2.1. Table of list of materials
2.2. List of apparatus
2.3. Procedure
3. Data and calculations 3.1. Record of all relevant raw data 3.2. Calculations with statistical manipulations
4. Results and discussion 4.1. Interpretation of data and comparison of results with known values 4.2. Discussion of the significance of the results 4.3. Was the original aim achieved 4.4. Conclusion
5. References

1. Introduction
1.1. Aim
To determine the kinetic parameters known as Vmax and Km of Alkaline Phosphatase. This will be done by determining and investigating the optimum pH and …show more content…

For a substrate to be converted into a product, enzymes must collide with a substrate and bind to its active site. As the temperature increase, the number of collisions per unit time increases which in turn increases the kinetic energy of the protein. This increases the chances of the substrate to successfully collide with an enzyme. Thus the rate of the reaction will also increase. When the temperature gets too high, the increase in Kinetic energy causes a lot of vibrations in the enzyme leading to the hydrogen bonds breaking. The shape of the active site on the protein now changes. The enzyme’s intra- and intermolecular bonds are broken causing the enzyme structure to denature (break down). (1) (3)
. Ionic interactions between positively and negatively charged amino acids hold enzymes together. The ionization state of amino acids (acidic of basic) can be affected by a change in the pH in which the enzymatic reaction occurs and are sensitive to hydrogen ion concentration. The majority of enzymes function over a small pH range. When pH is altered the rate of enzyme reaction reduce considerably and the balance between positively and negatively charged amino acids are shifted. Acidic amino acids contain a carboxyl functional group in their side chains whereas basic amino acids contain an amine functional group in their side chains. When ionization state of amino acids are altered the ionic bonds which determine the

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