Answer
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Hint: Trypsin is an enzyme that cleaves peptide bonds in proteins.
Pepsin is a proteolytic peptidase that cuts the peptide bonds of non terminal amino acids.
Complete Answer:
i) Trypsin is a serine protease enzyme that is found in the digestive system. Trypsin carries out the hydrolyzation of proteins. Trypsin is an enzyme that is formed in the small intestine. Trypsinogen is the proenzyme form of trypsin and is formed in the pancreas. Trypsin is activated in the small intestine from trypsinogen. The main function of trypsin is the splicing of peptide chains mainly at the carboxyl side of amino acids like lysine and arginine.
ii) Pepsin belongs to Endopeptidases. It breaks down proteins into small peptides. Pepsin is produced and secreted by the gastric chief cells present in the stomach lining. Pepsin is one of the main digestive enzymes in the digestive systems of many animals. Pepsin plays a major role in the digestion of food. Pepsin is an aspartic protease, i.e. it is a catalytic type of protease enzyme that uses activated water molecules to catalyze the peptide substrate. Pepsinogen is the proenzyme of pepsin. Pepsinogen is secreted by the gastric chief cells in the stomach lining. Pepsinogen activates and becomes pepsin after mixing with the hydrochloric acid present in the gastric juice.
Note:
1. Trypsin can be used in many biotechnological processes. Trypsin proteolysis is the digestion of proteins by trypsin. It is also known as trypsinization.
2. Pepsin and trypsin are two of the three principal proteases in the human digestive system, along with chymotrypsin.
Pepsin is a proteolytic peptidase that cuts the peptide bonds of non terminal amino acids.
Complete Answer:
i) Trypsin is a serine protease enzyme that is found in the digestive system. Trypsin carries out the hydrolyzation of proteins. Trypsin is an enzyme that is formed in the small intestine. Trypsinogen is the proenzyme form of trypsin and is formed in the pancreas. Trypsin is activated in the small intestine from trypsinogen. The main function of trypsin is the splicing of peptide chains mainly at the carboxyl side of amino acids like lysine and arginine.
ii) Pepsin belongs to Endopeptidases. It breaks down proteins into small peptides. Pepsin is produced and secreted by the gastric chief cells present in the stomach lining. Pepsin is one of the main digestive enzymes in the digestive systems of many animals. Pepsin plays a major role in the digestion of food. Pepsin is an aspartic protease, i.e. it is a catalytic type of protease enzyme that uses activated water molecules to catalyze the peptide substrate. Pepsinogen is the proenzyme of pepsin. Pepsinogen is secreted by the gastric chief cells in the stomach lining. Pepsinogen activates and becomes pepsin after mixing with the hydrochloric acid present in the gastric juice.
Note:
1. Trypsin can be used in many biotechnological processes. Trypsin proteolysis is the digestion of proteins by trypsin. It is also known as trypsinization.
2. Pepsin and trypsin are two of the three principal proteases in the human digestive system, along with chymotrypsin.
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