how HCl activates pepsinogen?
how HCl activates pepsinogen?
- HCL activates pepsinogen to its active form pepsin. How? Simple.
- HCL is a very strong acid. It cleaves (breaks) the ‘extra polypeptide’ of pepsinogen which was masking the active site.
- Pepsinogen has been activated and is now called pepsin.
2. HCl being a very strong acid, is responsible for the denaturation of proteins. And thus, make the role of pepsin more efficient. How? Simple…
(There're several bonds other than peptide binds in a protein like H-bond, electrostatic bond etc to make a protein more stable. Denaturation simply means breaking of all the other bonds except peptide bond)
Thus, denaturation of protein exposes peptide bonds (because it breaks all other bonds) and therfore pepsin can now act more efficiently.
Role of pepsin:
It simply cleaves the peptide bonds and converts, rather breaks, long polypeptide chains to smaller polypeptide chains.
But pepsin doesn't do all the work. To its MAXIMUM extent, it breaks the polypetide chains upto dipeptide level.(that too rarely)
It means, pepsin doesn't break proteins upto the level of free amino acids. (it is done later by intestinal and pancreatic enzymes).
Thus, protein is not digested to its absorbable form (amino acids) in stomach (by pepsin).
Hope it hepled.
- HCL activates pepsinogen to its active form pepsin. How? Simple.
- HCL is a very strong acid. It cleaves (breaks) the ‘extra polypeptide’ of pepsinogen which was masking the active site.
- Pepsinogen has been activated and is now called pepsin.
2. HCl being a very strong acid, is responsible for the denaturation of proteins. And thus, make the role of pepsin more efficient. How? Simple…
(There're several bonds other than peptide binds in a protein like H-bond, electrostatic bond etc to make a protein more stable. Denaturation simply means breaking of all the other bonds except peptide bond)
Thus, denaturation of protein exposes peptide bonds (because it breaks all other bonds) and therfore pepsin can now act more efficiently.
Role of pepsin:
It simply cleaves the peptide bonds and converts, rather breaks, long polypeptide chains to smaller polypeptide chains.
But pepsin doesn't do all the work. To its MAXIMUM extent, it breaks the polypetide chains upto dipeptide level.(that too rarely)
It means, pepsin doesn't break proteins upto the level of free amino acids. (it is done later by intestinal and pancreatic enzymes).
Thus, protein is not digested to its absorbable form (amino acids) in stomach (by pepsin).
Hope it hepled.
