During the process of digestion, the complex large molecules of protein are broken down into dipeptides and amino acids. These dipeptides and amino acids are further absorbed by the villi, present in the wall lining of the small intestine. The absorbed amino acids are further transported by the blood to various parts of the cell. Moreover, the amino acids can also be resourced from the degradation of defective and unnecessary cellular proteins.
The digestion of protein takes place in the stomach and duodenum (part of the intestine). The digestion of protein includes three primary enzymes. These are pepsin, trypsin, elastase chymotrypsin, and carboxypeptidase. Other enzymes are exopeptidase and dipeptidases. The protease enzyme trypsin and chymotrypsin are secreted by the pancreas whereas, the protease enzyme pepsin is secreted by the stomach. Therefore, it is concluded that the digestion of protein takes place in two steps: the first step is in the stomach and the second step is in the duodenum, small intestine. The amino acids are utilized by cells for repairing damaged tissues, for building body muscles, that is why protein or amino acids are also called building blocks of life.
The extra amounts of amino acids are stored in the form of glucose or ketones. During starvation, this stored amino acid is utilized to produce energy, since it can also be used as an energy source. The process of obtaining energy from protein or amino acids is called the Krebs cycle or TCA cycle. The TCA cycle stands for the tricarboxylic acid cycle; it is also called as the citric acid cycle .
Protease Enzymes in Digestion of Amino Acids
The protease enzymes which are involved in the digestion of proteins are pepsin, trypsin, elastase chymotrypsin, carboxypeptidase, or other enzymes such as exopeptidase and dipeptidases.
Enzymes Pepsin: Pepsin is a protease enzyme that is secreted by gastric chief cells that lines the stomach wall. The inactive form of pepsin is pepsinogen. After the secretion of pepsinogen, the pepsinogen is activated by acids presents in the stomach into its active form, pepsin. The pepsin is an endopeptidase, which breaks the protein into small peptides. The pH of pepsin is highly acidic. The pH of the pepsin lies between 1 to 4. The pepsin breaks down the peptide by catalyzing the peptide bond which is held together with the molecules of amino acids. The process of catalyzing the bound is called hydrolysis.
Enzyme trypsin: The trypsin enzyme is a medium-size globular protein. The trypsin enzyme hydrolyses the peptide bounds by cleaving from the C â€“ terminal side of the amino acids especially the residue of lysine and arginine amino acids. The inactive form of the trypsin enzyme is trypsinogen. It is secreted by the pancreas, secreted into the small intestine through the bile duct.
Enzyme chymotrypsin: The chymotrypsin enzyme is a proteolytic enzyme. It breaks the peptide bond of amino acids by the process of hydrolysis. It is a very slow reaction especially in the absence of a catalyst. Moreover, it is also used in drug discovery. It is also referred to as serine endopeptidase. The chymotrypsin enzymes are produced by acinar cells present in the pancreas.
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