Chymotrypsin

Definition

Chymotrypsin is a digestive enzyme produced in the pancreas that plays a crucial role in breaking down proteins into smaller peptides in the small intestine. It is a type of serine protease that specifically targets aromatic amino acids, aiding in protein digestion and nutrient absorption.

5 Must Know Facts For Your Next Test

1. Chymotrypsin is secreted as an inactive precursor called chymotrypsinogen and is activated by trypsin in the small intestine.
2. This enzyme primarily cleaves peptide bonds on the carboxyl side of aromatic amino acids such as phenylalanine, tryptophan, and tyrosine.
3. Chymotrypsin works optimally at a slightly alkaline pH, which is achieved when chyme enters the small intestine from the stomach.
4. The activity of chymotrypsin can be affected by various factors such as temperature, pH, and the presence of inhibitors that can block its function.
5. Deficiencies in chymotrypsin can lead to malabsorption issues, as proteins may not be adequately broken down for absorption in the intestines.

Review Questions

• How does chymotrypsin contribute to protein digestion in the small intestine?
  • Chymotrypsin contributes to protein digestion by breaking down complex proteins into smaller peptides, making them easier to absorb. It specifically targets peptide bonds adjacent to aromatic amino acids, effectively reducing proteins into forms that can be further processed by other enzymes. This function is essential for efficient nutrient absorption as it helps ensure that dietary proteins are sufficiently digested.
• Compare and contrast the roles of chymotrypsin and trypsin in the digestive process.
  • Both chymotrypsin and trypsin are pancreatic enzymes involved in protein digestion but have distinct roles and specificities. Trypsin activates chymotrypsin from its inactive form chymotrypsinogen and primarily cleaves peptide bonds after basic amino acids like lysine and arginine. In contrast, chymotrypsin specifically targets aromatic amino acids. Together, they complement each other's action, ensuring comprehensive protein breakdown.
• Evaluate the impact of pH on the activity of chymotrypsin and its implications for digestive health.
  • The activity of chymotrypsin is significantly influenced by pH, with optimal function occurring at a slightly alkaline level found in the small intestine. If the pH is too low or too high, chymotrypsin may become less effective or inactive, leading to inadequate protein digestion. This could result in malabsorption issues, which could further affect overall health by limiting nutrient availability and leading to deficiencies if protein intake is not properly digested.

Related terms

Protease: An enzyme that catalyzes the breakdown of proteins into smaller polypeptides or amino acids.

Trypsin: Another digestive enzyme produced by the pancreas, which activates chymotrypsin and also breaks down proteins but has a different specificity compared to chymotrypsin.

Pepsin: A digestive enzyme found in the stomach that begins protein digestion by breaking down proteins into smaller peptides before they enter the small intestine.