We often see advertisements claiming that enzyme foods are good for our health, but in reality, simply consuming enzymes is not enough to promote bodily functions. This article explains the actual functions and mechanisms of enzymes, corrects misconceptions about enzyme foods, and suggests the right way to take care of your health.
“Enzymes are so good for you?” is a common advertising phrase we see in newspaper articles and internet media. It lures consumers into thinking that all they need to do is take enzymes to strengthen their stomachs and heal their aches and pains. Most people buy and consume dietary supplements like enzyme foods to improve their health. Enzymes are advertised as a panacea, with claims that they can help with fatigue, weight loss, and even anti-aging. While this seems like an easy choice for consumers to make to address their health concerns, the science behind their effectiveness is often lacking. The truth is, taking enzymes doesn’t promote overall body function. Taking enzymes is just like taking a chunk of protein. In order for enzymes to function properly, chemical changes must occur where they are needed and according to the mechanism. However, the average person who doesn”t know this specialized science is likely to buy enzyme foods that claim to be good for you without question and at a high price. This problem stems from the asymmetry of health-related information in the modern world, where consumers are easily misled by hype and misinformation. Therefore, in this article, we”ll explain the function of enzymes, their mechanisms, and the different types.
As we’ve already mentioned, enzymes are obviously protein masses. Enzymes are globular proteins made up of a large number of amino acid residues. Humans have 23 pairs of homologous chromosomes with different sequences of DNA, which makes them biologically diverse. Similarly, enzymes are chains of amino acids that are linked and twisted to create structures and activate to do their job. For example, what you look like is influenced by the genes you inherit from your parents. Similarly, the structure of the digestive enzyme pepsin is shaped so that it can receive an amino acid sequence from tRNA and break down proteins in the stomach. The structure and function of these enzymes are important because they are more than just proteins; they are essential catalysts in the complex metabolic processes of life.
Enzymes bind to a substrate, or reactant, to form an enzyme-substrate complex and lower the activation energy of a chemical reaction so that the reaction can occur. Activation energy is the minimum energy required for a chemical reaction to occur, and by lowering this barrier, enzymes make it easier for reactants to change into other substances. In our example, pepsin, which helps digest proteins, binds to proteins and breaks them down into smaller units, called polypeptides. Instead of climbing a high mountain, the enzyme creates a lower hill to climb. This allows the chemical reaction to proceed more efficiently. However, pepsin isn’t the only type of enzyme in the body. To categorize them, an international consensus has been established based on the type of catalytic reaction they catalyze. There are six main categories, and the enzymes are classified according to their numbers EC 1: Redox enzymes. EC 2 is a group of functional group transferases. EC 3 are hydrolytic enzymes. EC 4 are degrading enzymes. EC 5 is an isomerase. EC 6 is a linking enzyme that binds two molecules together in a covalent bond. Each enzyme plays a role in many digestive and metabolic processes, and also contributes to waste elimination, detoxification, and sterilization. Each enzyme has a specific place in the body where it is produced and acts, and certain enzymes can cause excesses or deficiencies if they are present in the body in higher or lower amounts than they should be. This is why taking enzymes may not help. If you take enzymes from somewhere other than your gastrointestinal tract, it’s difficult for them to pass through the digestive tract and into the blood, because enzymes are proteins and are broken down into amino acids when absorbed.
Each type of enzyme has a different structure and catalyzes only one or very similar reactions in the body. This phenomenon is called enzyme substrate specificity. The idea is that an enzyme has a specific active site based on its structure, and the reaction occurs when the right substrate binds to its conformation. In the past, this property was explained by the key-lock model. As the old saying goes, “everything has a match,” and each of the many locks called substrates has a corresponding enzymatic key. However, there was a logical contradiction in this concept: it explained that enzymatic reactions were specific, but it did not explain how they could be facilitated by lowering the activation energy. So a new theory emerged: the induced fit theory. It says that the substrate doesn’t have a structure that exactly fits the active site of the enzyme, but when it binds, the enzyme slightly changes the structure of the active site, forming a complex. It’s like a man and a woman meeting. Let’s say a man and a woman are attracted to each other because they have something in common. When they get married and try to create a conjugal community, the enzymes show us how to create a conjugal community. When they are together, they may have grown up in different environments and have conflicts in their lifestyles. If you think of marriage as a chemical reaction, and the enzyme is a man and the temperament is a woman, it’s not easy to accept each other as they are. However, if you understand the differences and try to adapt your personality slightly to your partner’s, you can get much closer and make marriage easier. This interaction between enzymes and substrates plays a key role in important metabolic processes within living things.
However, just as there are interferers in relationships between men and women, there are also enzyme inhibitors that reduce the rate of reaction between enzymes and substrates. There are two main types of enzyme inhibitors. Competitive inhibitors and non-competitive inhibitors, which literally describes their role. Competitive inhibitors compete with the substrate for the enzyme’s active site. Non-competitive inhibitors bind to other sites on the enzyme and alter the shape of the active site, preventing it from binding to the substrate. It’s easy to understand this by analogizing it to human relationships. If we go back to the relationship between a man and a woman, an enzyme inhibitor is an interfering agent that ruins the relationship between them. Two women, substrates, and competitive inhibitors fight for the same man. This lowers the odds that the female temperament and male enzyme will fall in love. And even if the female temperament and male enzyme are compatible, the non-competitive inhibitor will act to break up their relationship in indirect ways, such as through the inevitable emigration abroad. As such, enzyme inhibitors interfere with the activity of enzymes and play an important role in regulating or inhibiting the rate of certain reactions in the body.
Enzymes are essential in the body to maintain homeostasis and keep the body working with normal mechanisms. As mentioned above, enzymes act in specific locations, undergo various competitive reactions, and react with suitable substrates. This is why people take digestive enzymes as nutraceuticals to help their digestive system function. However, I hope this article dispels the myth that enzymes will cure all diseases in the body. Finally, it”s important to remember that a balanced diet and proper exercise are more important than enzyme supplements to maintain a healthy life. It’s important to learn how to condition and take care of your body so that it can produce as much enzyme as it needs, rather than supplementing with additional enzymes.
