PROTEASES (or peptidases): hydrolytic enzymes involved in protein digestion.With their action, proteases are able to break the peptide bonds that unite the various amino acids and from whose repeated concatenation the protein molecules originate.
ORIGIN
- Pepsin: produced by the peptic cells of the stomach in an inactive form (pepsinogen). Activated by hydrochloric acid. It mainly intervenes on peptide bonds that engage aromatic amino acids (such as tyrosine, tryptophan and phenylalanine).
- Trypsin: produced by the exocrine pancreas in an inactive form (trypsinogen). Activated by duodenal enteropeptidase. It mainly intervenes on the peptide bonds that engage basic amino acids (such as arginine and lysine)
- Chymotrypsin: produced by the exocrine pancreas in an inactive form (chymotrypsinogen). Activated by trypsin. It mainly intervenes on the peptide bonds that engage aromatic amino acids (such as tyrosine, tryptophan and phenylalanine).
- Elastase: produced by the exocrine pancreas in an inactive form (pre-pro-elastase). Activated by trypsin. The only enzyme capable of attacking elastin and as such very important for the digestion of meat foods.
- Carboxypeptidase: produced and secreted by the exocrine pancreas in part in active form and in part in inactive form. They act on the peptide bonds placed at the carboxyl end of the amino acid chain.
- Aminopeptidases: produced and secreted by the duodenal mucosa. They intervene on the peptide bonds placed at the carboxyl end of the amino acid chain.
- Dipeptidases: secreted by enterocytes of the small intestine, they hydrolyze the peptide bond that holds single pairs of amino acids together
Proteases used for the digestion of food-borne proteins represent only a small part of the large family to which they belong. If we think that enzymes, like many hormones, are molecules of a protein nature, we realize how important the role played by proteases is. What better way to regulate the activity of these molecules than to degrade them if necessary by means of specific proteases? Here then is that the cells of the immune system contain proteases to digest the cell membrane of foreign microorganisms, which in turn (we are talking about bacteria) have on the one hand the ability to secrete proteolytic enzymes to invade the cell and on the other to release protein toxins (exotoxins) from which we must defend ourselves. Some plasma proteases, such as antithrombin III and plasmin, play an important role in coagulation, preventing an "excessive activation of this mechanism, which is instead enhanced by thrombin (which also belongs to to the large family of proteases).
The modulatory action of proteases is therefore fundamental in the regulation of various bodily functions; if, for example, abnormal proteins originate from protein synthesis, it is very important that they are degraded as soon as possible. Similarly, in wound healing, scar tissue cannot grow to infinity, but it must be limited by specific proteases. Furthermore, if we consider that proteases degrade and destroy protein molecules, we must expect that there are factors, including other proteases, capable of regulating their function and thus preventing the exalted proteolytic phenomena end up "causing damage to the tissues of the" organism.
Proteolytic phenomena affecting the muscle fibers are activated by fasting and prolonged physical exercise in order to produce energy and glucose starting from some glucogenic amino acids.
Plant proteases are also synthesized by plants in order to defend against pathogens, degrade peptides and modify the structure and function of other proteins. The pineapple stalk (bromelain), papaya (papain) and sprouted seeds (barley malt) are particularly rich in it. The ingestion of these foods or their extracts helps to regulate digestive function, assisting the action of endogenous proteases released in the digestive tract.
