Mention any two difference between pepsin and trypsin ?

Question

Answer

Two differences b/w trypsin and pepsin are :-

(i) Pepsin is secreted by the gastric glands of the stomach whereas the trypsin is secreted by the exocrine glands of the pancreas.

(ii) Pepsin functions in an acidic medium while trypsin functions in an alkaline medium.

hope it helps u..

Answer

Pepsin is secreted by gastric gland where as trypsin issecreted by exocrine gland of pancreas pepsin functions in acidic medium where as trypsin functions in alkaline medium

Answer

Pepsin:1.It acts in stomach.2.It acts in acidic medium.Trypsin:1.It acts in small intestine.2.It acts in alkaline medium.

Answer

Pepsin works in acidic medium but trypsin works in basic medium

Answer

Pepsin is produced in stomach while Trypsin is produced in pancreas.

Answer

Nice answer wait please

Answer

1. pepsin is secreted by stomach and Trypsin
by pancreas.
2. pepsin digest protein active only in presence of acid but trypsin digest protein.

Answer

Two Differences between Pepsin and Trypsin:

Pepsin and trypsin are both digestive enzymes that play crucial roles in the breakdown of proteins. However, they differ in terms of their site of action, specificity, and activation. Let's explore two key differences between pepsin and trypsin in detail:

1. Site of Action:
Pepsin primarily acts in the stomach, while trypsin functions in the small intestine.

- Pepsin: Pepsin is secreted as an inactive zymogen called pepsinogen by the chief cells of the gastric glands in the stomach. When pepsinogen comes into contact with the acidic environment of the stomach, it gets converted into its active form, pepsin. Pepsin works optimally at low pH levels (around pH 2) and is responsible for the initial hydrolysis of dietary proteins into smaller peptides.
- Trypsin: Trypsin, on the other hand, is secreted as an inactive zymogen called trypsinogen by the pancreas into the duodenum, the first part of the small intestine. Trypsinogen is activated by an enzyme called enterokinase, which is produced by the intestinal lining. Once activated, trypsin can catalyze the hydrolysis of peptide bonds, breaking down proteins into smaller peptides and amino acids.

2. Specificity:
Pepsin and trypsin exhibit different specificities towards the peptide bonds they cleave.

- Pepsin: Pepsin exhibits broad specificity and primarily cleaves peptide bonds adjacent to aromatic amino acids, such as phenylalanine, tyrosine, and tryptophan. Pepsin can also cleave bonds next to leucine, glutamic acid, and aspartic acid residues. This specificity allows pepsin to degrade a wide range of proteins into smaller peptide fragments.
- Trypsin: Trypsin, on the other hand, displays a more specific cleavage pattern. It hydrolyzes peptide bonds adjacent to basic amino acids, particularly lysine and arginine. Trypsin does not cleave peptide bonds adjacent to proline, which differentiates it from other proteases. This specificity enables trypsin to generate peptides with basic residues at the N-terminus.

In conclusion, pepsin and trypsin differ in terms of their site of action, specificity, and activation mechanisms. Pepsin primarily functions in the stomach, exhibits broad specificity, and is activated by the acidic environment. On the other hand, trypsin acts in the small intestine, displays a more specific cleavage pattern, and requires activation by enterokinase. Understanding these differences helps us appreciate the diverse roles these enzymes play in the digestion of proteins within the gastrointestinal system.

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