Nucleic acid cleaver | Pancreatic enzymes

Nucleic acid cleaver

The nucleic acid cleavers deoxyribonucleases and ribonucleases are enzymes that can cleave DNA and RNA. In humans, ribonuclease one is one of them. This is produced in the pancreas and cleaves the ester bond between a phosphate group and a hydroxyl group. Since all living organisms, both plants and animals, store their genetic information in DNA and RNA, these structures are also found in our food and must be broken down by enzymes.

Protein splitter

The pancreas also produces protein-splitting enzymes and their precursors. Proteins refer to all food components that are composed of amino acids. The complete chains of amino acids cannot be utilized by the human body, the amino acids must be cut apart.

Trypsin is produced as a precursor in the pancreas and is released together with an inhibitor to protect the pancreas. Trypsin is an enzyme that cuts particularly well behind basic amino acids. In addition to its own activity, trypsin can also activate other enzymes.

These include chymotrypsin, a serine protease that cleaves particularly aromatic amino acids. The preliminary stage of chymotrypsin is also produced in the pancreas and is only activated in the intestine. An increased concentration of chymotrypsin in stool can be an indication of pancreatic disorders.

Both trypsin and chymotrypsin have their pH optimum in the range of seven to eight and thus in the slightly alkaline range. Another enzyme whose precursor is produced in the pancreas is elastase. The elastase is also activated by trypsin.

It is a protein-splitting enzyme. The pancreatic elastase is excreted unchanged with the stool after production and can therefore be used as a safe marker for a disease or underfunction of the pancreas. Increased production of elastase can lead to lung damage.

Collagen is found in the connective tissue of many living organisms and can be broken down by collagenases. Collagenases are protein-splitting enzymes, so-called peptidases. In humans, most collagenases are metalloproteases.

These collagenases are dependent on certain metal ions to perform their function. Some bacteria also possess collagenases. In this way, for example, clostridia can destroy the connective tissue in the intestine.

Kallikrein is a serine protease and thus a protein-splitting enzyme that has many tasks in the body. There is a precursor of kallikrein in the blood and this has an influence on blood clotting. Kallikrein also affects blood pressure and the body’s water and salt balance.

Kallikrein is also involved in inflammatory processes. It is produced in the pancreas, the oral salivary glands and the kidneys. About fifteen subtypes of Kallikrein are known.

Some of these subtypes can also be determined as tumour markers. Carboxypeptidases belong to the protein-splitting enzymes that are produced in the pancreas. They are activated in the intestine by the enzyme trypsin.

After this activation, carboxypeptidases split off amino acids from the end of the amino acid chains in food. Carboxypeptidase A splits the amino acid chain into aromatic amino acids and carboxypeptidase B into basic amino acids. Carboxypeptidases thus help to make the proteins in the food usable for the body.