Enzymes are used to speed up biochemical reactions within your body by lowering the energy level necessary to initiate the reactions. They are proteins composed of amino acids, each type with its own highly specific purpose. They can do thousands of similar reactions because they are not altered during the catalyzing process. Enzymes have the ability to both build and disassemble cells although it is not known exactly how they do their job.

J. Robert Lemon calls enzymes the "biochemical agents of life". They can be found throughout your body (and those of all plants and animals) and are essential for nearly every metabolic process. They are required for regulating digestion, hormone production, the immune system, energy production and even cell recycling.

Most enzymes are manufactured within the body, the rest must be consumed. They are extremely sensitive to heat (at 100C/212F all enzymes are dead), which is why your Health teacher tells/told you to eat your fruit and veggies raw.

Raw meat consumption is frequently being linked to longer life and less chance of chronic diseases. Enzymes have also been used in the treatment in a wide range of medical problems including HIV, obesity and prostate cancer. They are used in the creation of a wide variety of unlikely products such as detergents, pulp/paper and textiles.


20030501: Props to Oolong for a correction in the definition of enzymes. He also pointed out a wicked metanode that BaronWR wrote up.

The most important thing to remember about enzymes are that they are catalysts, which means that they make chemical reactions happen faster.

I know a chemical engineer who used to be in the petrochemical industry. He used to design and build large plants for cracking and separating the components of crude oil then converting them to other useful compounds. The catalysts they used typically only worked at extreme temperatures and pressures. It never ceased to amaze him how biological enzymes did pretty much the same thing at body temperature and atmospheric pressure.

While I agree with dustfromamoth that eating more raw food (well, mainly fruits and vegetables ... and the occasional sashimi) is good for you, there is no medical evidence that your pancreas will die off faster because you cook your food rather than eat raw food.

In fact, there is no evidence whatsoever that the human body has "enzyme potential" that will run out if you don't eat raw food once in a while. In any case, if you eat meat, the only enzymes that the meat will contain are, I assure you, not the kind of enzymes that will digest the meat itself for you. Be wary of disinformation, especially when it's packaged nicely.

Enzymes are quite literally, the colossal difference between raw and cooked foods. They are delicate yet powerful biochemical catalysts. They are destroyed by temperatures over 118 degrees Fahrenheit, which means that they do not even survive light steaming, sadly. I say sadly because they speed burning or building reactions in the body, according to need. They are basically specialized proteins, usually with complex names ending in the suffix -ase. Protease digests protein, lipase digests fats (lipids), and amylase digests carbohydrates. Amylase comes from the salivary glands; carbs begin their digestion right in your mouth. In fact it is rather imperative that you chew thoroughly, as they say in Tao, “Drink your foods and chew your liquids”. The enzymes in your digestive tract are not sufficient enough for optimal digestion. This is why you may feel sluggish after consuming starches.
Lipase is produced mainly in the liver and protease, from the pancreas. Although these organs continue to function over the entire course of a healthy life, the gradually wear down, most especially with typical American diets. A study at the University of Minnesota has shown that rats fed for 135 days on an 80 percent cooked food diet resulted in an increase pancreatic weight of 20 to 30 percent. Which means that the pancreas is forced to work harder with a cooked food diet. The director of this study says that although the body can manufacture enzymes, the more you use your enzyme potential, the faster it will ‘run out’. An eighteen year old may produce amylase levels 30 times greater than those of an 85 year old person, for example.

Enzymes are what make seeds sprout. Sprouts are, in fact, one of the richest sources of enzymes. Some equally excellent sources are papaya, pineapple and the aspergillus plant. Only raw food has functional "live" enzymes. Therefore the liver, pancreas, stomach and intestines must come to the rescue and supply the necessary digestive enzymes to an individual nourished solely on a cooked food diet. As you could imagine, this extra activity can be very detrimental to health and longevity because it continually taxes the reserve energy of our vital organs. Moreover, cooked food passes through the digestive tract far more slowly than raw, and it tends to ferment. This throws poisons back in the body.

Virtually all degenerative diseases are caused or aggravated by digestive problems. This statement is backed up by the most extensive study ever undertaken by the US government, in its 1978 report “Diet and Killer Diseases”. Enzymes, I tell you! Enzymes are essential for a prolonged (and wholesome) existence! Eat more raw foods. Or, a good habit to get into: if you must eat something heavily cooked, e.g. a steak, eat a fresh salad beforehand, to place some enzymes in your stomach to hlep digestion along.

Update: atesh asked me if this includes raw meat. Yes it does!

Obligatory disclaimer, due to numerous (and sometimes heated) complaints: I am not claiming absolute authority over this topic. I am simply re-stating some of the ideas i have read in health oriented books. I shall name the titles of these once they are returned from my friend down the street.

Enzymes are biological catalysts. The job of an enzyme is, generally, to speed up a chemical reaction. Enzymes do this by providing a lower energy route for a reaction, so the reaction can occur at a lower temperature, but the reaction speed can be fast.

Enzymes are complex proteins, and they are very specific about the temperatures at which they work. At temperatures cooler than this, the enzyme will work slowly. Much above the optimum, and the protein will change shape, and will stop working permanently. This is called denaturing. pH (acidity) is also a contributing factor, and this has an absolute optimum value as well.

Enzymes are specific to a single reaction. This reaction takes place on a special active site on the protein.

Enzymes are said to work by 'lock-and-key' theory. Some enzymes collect two or more reactant 'keys', and join them together, while others do the reverse. Chemicals changed by an enzyme are called substrates.

Our bodies contain hundreds of thousands of different enzymes, in every living cell of our bodies. We need enzymes to live as we do - life would be really impractical if we had no enzymes to help us.

Finally, it should be mentioned that enzymes are able to be released at given quantities, giving good control over reaction speeds in the body.

In every living organism, chemical reactions take place within every cell, called metabolic reactions. These reactions are mostly controlled by biological catalysts called enzymes. Enzymes can both break down molecules, such as salivary amylase which breaks down starch; and make large molecules from smaller ones, such as starch phosphorylase, which builds up starch in plants. Enzymes tend to be used a lot in digestion, which is the breakdown of large molecules into smaller molecules the body can absorb. Examples of these enzymes are protease, which breaks down proteins into amino acids, and carbohydrase which breaks down carbohydrates into simple sugars. Enzymes can also be found inside cells, such as catalase, which breaks down harmful hydrogen peroxide into water and oxygen.

In the course of a reaction involving an enzyme, one substance is changed into another. The substance present at the beginning is called the substrate, and the substance produced at the end is called the product. Enzymes themselves are all proteins, each with an exact shape. They also include a gap in the side of them, which is shaped so that the substrate molecule will fit into it. This gap or dent is called the active site. During the reaction, the substrate molecule fits into the active site, and the enzyme pulls at it and makes it split apart into the products. When the reaction has finished, the products leave the active site and the enzyme is ready to perform the reaction again.

Each enzyme has a specific shape of active site, and will only accept one type of molecule, so the enzymes are specialised depending on which reaction they have to perform. They can also only create products of a certain type for the same reason.

There are also other properties that all enzymes have, such as the conditions they work best in. Most enzymes work best at a temperature of about 37ºC. Usually, chemical reactions get faster the hotter the conditions are, because molecules move around faster and hit each other with more energy. However, because the enzymes are proteins, they are damaged by high temperatures, and once the temperature reaches about 40ºC the enzymes become denatured, and are no longer useful as catalysts. This is one of the reasons why the human body is kept at a temperature of 37ºC. As well as having an optimum temperature, enzymes also have an optimum pH at which they operate. Because they are proteins, they are damaged by very acidic or alkaline conditions. Therefore they work best at a pH of 7, or neutral.

Although enzymes facilitate and speed up reactions, they are not actually used up when the reaction takes place. This is because they are catalysts. Therefore the body does not need to replace them unless they become denatured by a high temperature or pH.

Inside the body is not the only place where enzymes can be found. They are also used for other purposes, such as in washing powders, and also in the food industry. If clothes are stained with substances from animals or plants, these substances are often made up of particles such as proteins or fats. The easiest way to remove these is by adding protease and lipase to the washing powder, which break down the proteins or fats causing the stain. If washing powders contain enzymes, they are called biological washing powders. Originally, they only worked at warm temperatures, because at anything above about 40ºC they became denatured. However, this problem can be avoided by using enzymes from bacteria that naturally live in hot areas such as hot springs.

In the food industry, enzymes are used for a variety of purposes. They can be used to help make fruit juice by breaking down the pectin in the fruit, a substance that helps stick plant cells together. If this is broken down, the fruit is easier to juice because it is softer. When enzymes are used for a function such as this, they are immobilised to stop them from getting in to the fruit juice itself. Since they are catalysts, and so can be used over and over again, to lose them in the fruit juice would be a waste. Therefore they are attached to a substance called alginate, which is like agar jelly. When the fruit juice is filtered off, the alginate is left behind, and the enzymes are attached to it.

The enzyme amylase is also used in the food industry to create sugar. Normally, sugar is obtained from sugar cane or beet. However it is possible to obtain it from starch by using amylase, which breaks up the starch into sugar. Plants containing starch, such as potatoes, are crushed with water, and then amylase is added. This then digests the starch to form maltose. Sugars can also be converted to different kinds of sugar by enzymes. For instance fructose, a sugar that is sweeter than glucose, can be obtained by adding isomerase to glucose.

Recently it has become possible to use enzymes as biosensors. A certain enzyme is used to catalyse glucose into hydrogen peroxide and an acid. This is useful when testing blood sugar levels. The change in oxygen level caused by the enzyme is detected by the biosensor, and produces an electrical output depending on the amount of oxygen detected. This can be measured, and displayed on a screen. This kind of biosensor is very useful for diabetics, who need to monitor their blood sugar levels. It makes use of the property the enzymes have of being specific. Since the enzyme only catalyses one type of molecule, in this case glucose, only changes in the glucose level will produce a response in the readout. Also, because enzymes are not used up, the biosensor never needs to be replaced.

Gritchka has also drawn my attention to another use for enzymes, this time in genetic research. In order for research to be carried out as to what certain genes do in a cell (a key step in research into HIV and AIDS, as one example), "molecular scissors" are used. More properly known as ribozymes, or catalytic RNAs, these scissors cut the RNA messages used to convey information from certain genes, so rendering the genes effectively useless.

I say enzymes when talking about ribozymes, but there seems to be some dissent as to whether ribozymes really count as enzymes, since they are not actually proteins (see above, where I say "Enzymes themselves are all proteins"(!) I suppose the problem occurs because when the term was defined, all such biological catalysts were proteins (ribozymes were discovered in 1987). It all really comes down to definition. If you define an enzyme as a biological catalyst, then ribozymes are enzymes. If you include being a protein in the requirements, then they are not. Either way, ribozymes exhibit enzyme-like properties, which is why they are included here.

En"zyme (?), n. [Pref. en- (Gr. in) + Gr. leaven.] Physiol. Chem.

An unorganized or unformed ferment, in distinction from an organized or living ferment; a soluble, or chemical, ferment. Ptyalin, pepsin, diastase, and rennet are good examples of enzymes.


© Webster 1913.

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