How the pH of Trypsin and Pepsin affect light transmission
Interpretation
From the graph the enzyme Trypsin has 51% light transmission at pH 2. At pH 9 the Trypsin has 39% light transmission. Between pH 2 and pH 9 the percentage of light transmission decreases at a steady rate, until it reaches pH 8 where there is a steep increase from 30% to 39% as the enzyme has reached its optimum pH at 8. During the experiment in the boiling tube this pH had the deepest red colour as the most protein gelatine was broken up. This meant that in the colorimeter when testing to see what the light transmission, this pH let the least light through. For this enzyme as the pH increases the percentage of light transmission decreases until it gets to pH 8 where it increases again to 39%.
From the graph the enzyme Pepsin has 26% light transmission at pH 2. At pH 9 the Pepsin has 49% light transmission. Between pH 2 and pH 9 the percentage of light transmission increases at a steady rate. For this enzyme the optimum pH is pH 2 as it has the lowest light transmission on the graph because we didn’t test pH 1 which may have had a lower percentage of light transmission. As the pH increases the percentage of light transmission also increases.
The optimum pH is the pH that the shape of the active site most complements the substrate. If you move away from the optimum pH the structure the active site of the enzyme are altered. Ionic bonds in the tertiary structure may be disrupted. This means that at different pHs the substrate attaches less readily to the enzyme. At the optimum pH the charges on the active site match those of substrate so an enzyme-substrate complex forms. At low and high pHs the charges on the active site repel the substrate which means there is less attachments. At extreme pHs the enzyme may be permanently denatured, this is because proteins fold into particular shapes that are vital for their function. The shape of a protein will fold into is determined by its amino acid sequence, since
From the graph the enzyme Trypsin has 51% light transmission at pH 2. At pH 9 the Trypsin has 39% light transmission. Between pH 2 and pH 9 the percentage of light transmission decreases at a steady rate, until it reaches pH 8 where there is a steep increase from 30% to 39% as the enzyme has reached its optimum pH at 8. During the experiment in the boiling tube this pH had the deepest red colour as the most protein gelatine was broken up. This meant that in the colorimeter when testing to see what the light transmission, this pH let the least light through. For this enzyme as the pH increases the percentage of light transmission decreases until it gets to pH 8 where it increases again to 39%.
From the graph the enzyme Pepsin has 26% light transmission at pH 2. At pH 9 the Pepsin has 49% light transmission. Between pH 2 and pH 9 the percentage of light transmission increases at a steady rate. For this enzyme the optimum pH is pH 2 as it has the lowest light transmission on the graph because we didn’t test pH 1 which may have had a lower percentage of light transmission. As the pH increases the percentage of light transmission also increases.
The optimum pH is the pH that the shape of the active site most complements the substrate. If you move away from the optimum pH the structure the active site of the enzyme are altered. Ionic bonds in the tertiary structure may be disrupted. This means that at different pHs the substrate attaches less readily to the enzyme. At the optimum pH the charges on the active site match those of substrate so an enzyme-substrate complex forms. At low and high pHs the charges on the active site repel the substrate which means there is less attachments. At extreme pHs the enzyme may be permanently denatured, this is because proteins fold into particular shapes that are vital for their function. The shape of a protein will fold into is determined by its amino acid sequence, since