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What Is Trypsin Digestion?

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  • Written By: C.B. Fox
  • Edited By: Susan Barwick
  • Last Modified Date: 17 October 2014
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Trypsin digestion occurs when long chains of protein are broken into smaller amino acid chains. The body then uses these amino acids in many different cellular processes. A class of enzyme called a protease, trypsin is a chemical that starts off in the pancreas as tryptonase. When tryptonase reaches the small intestine, it is broken down into its active form, trypsin, and is able to digest proteins.

Protein is an important component in many body functions. While the body is capable of recycling a large percentage of its daily protein needs from dead cells and enzymes that have completed their tasks, it requires additional protein in the form of digested foods. Proteases, including trypsin, are released into the digestive tract where they attack the bonds holding long protein molecules together.

The pancreas is responsible for manufacturing trypsin and releasing it into the digestive tract. Before it reaches the small intestine, it is inert so that it doesn’t damage the pancreas. Once it reaches its final location, the trypsin is activated. When trypsin digestion is complete, the trypsin enzyme itself is broken back down into amino acids and recycled.

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The environment in the stomach is highly acidic, which means the pH is below the neutral value of 7. This acidity helps to break chunks of food down into a paste. Once the food matter leaves the stomach and enters the intestine, however, the pH becomes slightly alkaline, or greater than 7. Trypsin digestion is most effective in environments where the pH of about 8.

Each type of protease is responsible for breaking down only specific types of proteins. Trypsin digestion dissolves the bonds only in the amino acids arginine and lysine. Though trypsin is molecularly quite similar to another protease formed in the pancreas, chymotrypsin, the two enzymes are not attracted to the same protein chains.

The study of trypsin digestion has been relatively easy because the enzyme is abundant and easy to extract and purify. By placing a protein in a sample of pure trypsin, scientists are able to see how quickly and efficiently the protease breaks down the protein into shorter amino acid chains. Experimentation on trypsin has led to discoveries that have made it easier to study enzymes that are less stable.

Of all the proteases, trypsin digestion singles out the fewest types of proteins. This quality is exploited by laboratory scientists, who use the protease to break down lysines and arginines. Trypsin breaks down these molecules in a predictable way, which helps scientists isolate certain amino acids in the lab.

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