Protease: benefits, dosage, contraindications

Proteolytic enzymes are a family of enzymes that hydrolyze peptide bonds in proteins or peptides. Proteolytic enzymes are present in all tissues, in cell membranes, the cytoplasm, and individual organelles. These enzymes can be endopeptidases, which hydrolyze peptide bonds within the protein, or exopeptidases, which cleave terminal amino acids. Proteolytic enzymes differ in the size of the substrate they degrade, the number and types of amino acids they cleave, their optimal pH for activity, and their localization in the organism. In the body, proteolytic enzymes play many roles, including the degradation of intracellular proteins, the control of physiologically active peptides, the presentation and recognition of antigens in the context of the cellular immune response, muscle remodeling and function, collagen turnover, digestion, blood coagulation... Pathological changes in proteolytic enzyme activity lead to inflammation, tissue damage and muscle wasting. In addition, changes in proteolytic enzyme activity are at least partly responsible for changes in muscle development that occur both as benefits and as side effects of certain drugs. The activity of a large number of proteases is controlled by cellular inhibitors. Inappropriate or pathological activity plays a role in various disorders, including joint inflammation, muscle degradation, including cachexia and sarcopenia, pulmonary disorders, and dementia. Proteolytic enzymes, as enzymes that break down proteins present in the body or on the skin, are consumed to promote digestion or the degradation of proteins involved in pain and inflammation.