Trypsin Investigation

Topics: Pancreas, Enzyme, Protein Pages: 4 (1049 words) Published: March 27, 2004
Science Coursework

Trypsin Investigation

Aim

I am going to prove that temperature effects the rate in which the enzyme Trypsin breaks down milk substrate into amino acids.

Investigation

"We strongly recommend the use of Vanish Stain Removal Tablets in

conjunction with a 900 spin wash at 70°C"

This was found on a milk carton of a well-known drinks company, Nesquick. The major food group constituent of milk is, of course, milk. For my Science Investigation, I am going to test different temperatures to see which dissolves the Nesquick substances quickest. The input variable is the temperature.

Prediction

Trypsin is an enzyme found in the pancreatic juices, which are secreted from the pancreas. It is produced to break down foods into smaller particles.

۵۵۵۵۵۵۵۵۵۵۵۵۵۵۵۵ ۵۵۵۵۵۵۵ ۵۵۵۵۵۵۵ ۵۵ ۵ ۵ ۵ ۵۵ ۵ ۵

Proteins Peptides Amino Acids

The cells in the human pancreas are made of protein, which enzymes digest, so you would expect the pancreas walls to be digested. However, enzymes are released inactive from the pancreas. Trypsin only becomes active when enterokinase is added. This allows complete break down in the ileum and duodenum.

I predict that the stains will be removed quickest at 37.5°C in alkaline conditions. I think this because these are the conditions they work in the human body. Enzymes allow the substrate to fit into it like a lock and key. The bond on the substrate is degraded and the substrate breaks at two. This reaction would happen between points A and B on the previous graphs.Milk substrate can fit exactly into the enzyme. This is where Proteins are broken into Peptides and then into Amino AcidsThe substrate will no longer be able to situate itself in the enzyme, therefore there will be fewer / no reactions and the process will take a lot longer. Therefore, the enzymes cannot breakdown the substrate chains. The enzyme will become denatured (mis-shaped) and therefore it wont have a lock and key fitting in which the...
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