INTRODUCTION
Trypsin is a proteolytic enzyme, important for the digestion of proteins. Enzymes are biological catalysts for metabolic process in cells. A catalyst is a substance that changes the rate of a reaction. Enzymes act as catalysts for chemical reactions in the body. Enzymes are large proteins that are not consumed or changed in a chemical reaction. They are highly specific to the substrate - the substance an enzyme acts on - they act upon. When an enzyme is available with an empty active site, the substrate binds to the enzyme. The substrate is converted into products and the products are released.
Your pancreas secretes trypsin as an inactive proenzyme called trypsinogen. Once in the intestine, an enzyme called enteropeptidase, which is secreted from intestinal cells, cuts off a small piece of trypsinogen to produce the active trypsin enzyme. Activated trypsin, in turn, helps break down food …show more content…
The aim of this study is to investigate the rate of efficiency of trypsin, in a milk solution, when varying the pH levels, and to record the light transmittance as the reactions proceed using a colourimeter. It is hypothesized that trypsin will break down the milk proteins (casein) to amino acids fastest in a buffer solution of pH 11, and slowest in a buffer solution of pH 4. These pH levels chosen in accordance to see the clear distinction between trypsins pH optima.
DISCUSSION
It was hypothesized that the trypsin solution would act more efficiently with the buffer solution of pH 11, due to the fact that lower pH’s would denature the effect of the enzyme. It is clearly obvious due to the graphs that there there is a slight significant difference. The distinction between the results were so minimal, however, the hypothesis was supported. This may be a result of pH 7 and pH 4 being below the trypsin pH
Trypsin is a proteolytic enzyme, important for the digestion of proteins. Enzymes are biological catalysts for metabolic process in cells. A catalyst is a substance that changes the rate of a reaction. Enzymes act as catalysts for chemical reactions in the body. Enzymes are large proteins that are not consumed or changed in a chemical reaction. They are highly specific to the substrate - the substance an enzyme acts on - they act upon. When an enzyme is available with an empty active site, the substrate binds to the enzyme. The substrate is converted into products and the products are released.
Your pancreas secretes trypsin as an inactive proenzyme called trypsinogen. Once in the intestine, an enzyme called enteropeptidase, which is secreted from intestinal cells, cuts off a small piece of trypsinogen to produce the active trypsin enzyme. Activated trypsin, in turn, helps break down food …show more content…
The aim of this study is to investigate the rate of efficiency of trypsin, in a milk solution, when varying the pH levels, and to record the light transmittance as the reactions proceed using a colourimeter. It is hypothesized that trypsin will break down the milk proteins (casein) to amino acids fastest in a buffer solution of pH 11, and slowest in a buffer solution of pH 4. These pH levels chosen in accordance to see the clear distinction between trypsins pH optima.
DISCUSSION
It was hypothesized that the trypsin solution would act more efficiently with the buffer solution of pH 11, due to the fact that lower pH’s would denature the effect of the enzyme. It is clearly obvious due to the graphs that there there is a slight significant difference. The distinction between the results were so minimal, however, the hypothesis was supported. This may be a result of pH 7 and pH 4 being below the trypsin pH