Question

The function of erepsin in the process of digestion is to convert
A. Fats into amino acids
B. Proteins into amino acids
C. Polysaccharides into saccharides
D. Disaccharides into monosaccharides

Answer 1

Erepsin is a protein and a mixture of enzymes found within the intestinal juices that digest peptones into amino acids. It’s produced and secreted by the intestinal glands within the ileum and also the pancreas, but it's also found widely in other cells.

Complete answer:
Proteins digestion takes place as:
Digestion within the gastric juice: Pepsin is a proteinase of digestive juice. It acts with the assistance of HCI and converts all digestible proteins up to the peptone stage. Proteolytic enzymes aside from pepsin (e.g., cathepsin, parapepsins, gastricsin) with the pH optima from 1.8—4.5 are present in digestive juice.

Digestion within the Pancreatic Juice: Trypsin is the protease of digestive fluid. Trypsin is secreted as inactive trypsinogen. It's activated by the action of enteropeptidase present within the succus entericus. Inactive trypsinogen can act on protamines and peptones slightly. Activation can even be led to by calcium salts.
Tryptic activity:
Proteins → alkali metaproteins → primary proteoses → secondary proteoses → peptones → polypeptides → lower peptides amino acids. Tryptic digestion ends and erepsin action begins.
Digestion within the Succus Entericus: Digestion of protein within the secretion depends upon the tryptic activity because the protease present within the secretion is unable to hydrolyse the protein.

Digestion of Nucleoproteins: The proteolytic enzymes, pepsin and trypsin, hydrolyse nucleoproteins into their protein and prosthetic part supermolecule components, within the commencement. Nucleic acids are depolymerized by the hydrolytic action of pancreatic ribonuclease and deoxyribonuclease with the production of oligonucleotides and pyrimidine mononucleotides. Digestion within the intestine takes place partly within the lumen by succus entericus.

Digestion of Casein (Milk): The chief protein of milk is casein, a posh phosphoprotein. Three constituents of milk require digestion:
Protein: Caseinogen, Lactalbumin and Lactoglobulin
Fats: They undergo the identical process of digestion as other fats.
Lactose: Digested by lactase to glucose and galactose.

Digestion of collagen and gelatin: Collagen is present in white plant tissue, tendons, bones, etc. Gelatin is ready from it by boiling with acid. Its digestion:
In the gastric juice: Collagen → gelatin → gelatoses → gelatin peptone.

Digestion of mucin: It is a glycoprotein. Digestive juice breaks it into glucosamine and peptone-like substances. The latter is further digested as other peptones. Glucosamine is maybe absorbed in and of itself.

Therefore, the answer is B, proteins into amino acids.

Note: Erepsin: Consists of a mix of enzymes (intracellular) including amino-peptidases and di-peptidases. Also, it acts best in a slightly alkaline medium, optimum pH is about 8.0.
It cannot act on native proteins. It acts upon lower peptides and converts them into amino acids.
It consists of the many different peptidases. The assorted peptidases act serially, one after the opposite, upon the smaller and smaller fragments of the peptide molecule. At each stage of digestion a unique peptidase comes into action.