Medicinal use of enzymes

چکیده مقاله

Introduction: Enzymes are important in therapeutic and commercial procedures because they accelerate a chemical reaction to produce a useful effect or product. The total number of pharmaceutical enzymes used worldwide is probably more than 3000 enzymes, counting tens of thousands of formulations containing different combinations of these substances. Most of the industrial enzymes, including the enzymes used in the pharmaceutical industry, are produced by fermentation of suitable microbial strains, mainly bacteria and fungi, due to their easy handling, fast growth rate, and appropriate scale in large vessels. Enzymes used as drugs have 2 important features that distinguish them from conventional drugs. 1) Unlike drugs, they bind and act on their targets with high affinity. 2) are highly specific and act as catalysts to convert multiple target molecules into desired products. These two properties turn enzymes into special and powerful drugs that can perform biochemical treatment in the body that the synthetic active ingredient cannot do. Several enzymes are used to prevent and treat common diseases such as heart attack and stroke, for example, collagenase enzyme is used to heal burn wounds and chondroitinase enzyme is used to treat spinal cord injury. Lysosomes are naturally used as an antibacterial agent in foods and consumer products, due to their ability to break the carbohydrate chains in the bacterial wall. It has also been shown that they have anti-HIV activities because they have RNaseA and RNaseU and selectively destroy viral RNAs, and they have presented exciting possibilities in the treatment of HIV infection. Methods: Chemical immobilization of proteins and enzymes was first performed in the 1960s and is an emerging approach for new drug therapies. Immobility means enzymes that have limited mobility or become less mobile due to chemical or physical treatment. The industrial use of enzymes is very limited, because they are very unstable, have a high purification cost, and after the completion of the catalytic process, they have a laborious process of recovering the active enzyme from the reaction mixture. Immobilized enzymes are more stable against pH, temperature stress and are less sensitive to denaturing agents. In addition, an immobilized (immobilized) enzyme should have long-term stability and unchanged biological activity and sensitivity compared to the free enzyme after binding to the matrix if used as a therapeutic target. Immobilization was used for studies with enzymes such as