what are enzymes

Enzymes are proteins

Like other protein, enzymes consist of long chains of amino acids held together by peptide bonds. They are present in all living cells, where they perform a vital function by controlling the metabolic processes whereby nutrients are converted into energy and fresh cell material.

Furthermore, enzymes take part in the breakdown of food materials into simpler compounds. Some of the best-known enzymes are those found in the digestive tract where pepsin, trypsin and peptidases break down proteins into amino acids, lipases split fats into glycerol and fatty acids, and amylases break down starch into simple sugars.

Enzymes are catalysts

Enzymes are capable of performing these tasks because, unlike food proteins such as casein, egg albumin, gelatine or soya protein, they are catalysts. This means that by their mere presence, and without being consumed in the process, enzymes can speed up chemical processes that would otherwise run very slowly, if at all.

After the reaction is complete, the enzymes is released again, ready to start another reaction. In principle, this could go on forever, but in practice most catalysts have a limited stability (lifetime), and sooner or later their activity becomes so low that it is no longer practical to use them. This is particularly true for enzymes, and most enzymes are therefore used only once and discarded after they have done their job.

Enzymes are specific

Contrary to inorganic catalysts such as acids, bases, metals and metal oxides, enzymes are very specific. In other words, each enzyme can break down or synthesize one particular compound. In some cases, they limit their action to specific bonds in the compounds with which they react. Most proteases, for instance, can break down several types of protein, but in each protein molecule only certain bonds will be cleaved depending on which enzyme is used. In industrial processes, the specific action of enzymes allows high yields to be obtained with a minimum of unwanted by-products

Enzymes are efficient

Enzymes are very efficient catalysts. For example, the enzyme catalase, which is found abundantly in the liver and in the red blood cells, is so efficient that in one minute one enzyme molecule can catalyze the breakdown of five million molecules of hydrogen peroxide to water and oxygen.

Enzymes are part of a sustainable environment

As mentioned earlier, enzymes are present in all biological systems. They come from natural systems and when they are degraded, the amino acids of which they are made can be readily absorbed back into nature.

Enzymes work only on renewable raw materials. Fruit, cereals, milk, fats, meat, cotton, leather and wood are some typical candidates for enzymatic conversion in industry, Both the usable products and the waste of most enzymatic reactions are non~toxic and readily broken down. Finally, Biotechnologic industrial enzymes can be produced in an ecologically sound way where the waste sludge, is recycled as fertilizer.

Enzymes work in mild conditions

Being formed to work in living cells, enzymes can work at atmospheric pressure and in mild conditions with respect to temperature and acidity (pH).

Most enzymes function optimally at a temperature of 30-70'C and at pH values which are near the neutral point (pH 7). For certain Cosmetic/OTC topicals technical applications, special enzymes have been developed that work at higher temperatures.

However, no regular enzyme can withstand temperatures above IOO'C for long but Campo has developed such high heat stable enzymes with genetic manipulation techniques from biotechnological plants with genetic cell-clone manipulation of RNA/DNA of Thermus aquatica ( thermal sulfur vent living organism) and Methanococcus sp. ( another organism surviving in the deep-ocean volcanic thermal trenches.

Enzyme processes are therefore potentially energy-saving and save investing in special equipment resistant to heat, pressure or corrosion.

Due to their efficiency, specific action, the mild conditions in which they work and their high biodegradability, enzymes are very well suited for a wide range of industrial applications.

Enzymes are at work in our bodies

You do not have to look far for a good example of enzymes at work. Just eat something.
One enzyme is already at work in your mouth while you chew A an alpha-amylase. Amylases break down starch into smaller sugars - dextrins and maltose. Typical starchy foods are potatoes, pasta and rice.

When the food reaches your stomach, acidic gastric juices start to flow from special glands.
An important component of these juices is the enzyme pepsin.

This is a protein-splitting enzyme and it works best in the conditions of high acidity found in the stomach.
The partly digested food and gastric juices are then churned around in your stomach and propelled into the duodenum.

It is here that another important part of digestion takes place. Pancreatic juice is released from the pancreas and this neutralizes the acid. An enzyme contained in the juice chops starch into its simplest sugars, and another breaks the protein down further into amino acids which are one of the main building blocks of all living matter.

So far, any fat has remained untouched, but now an enzyme made in the pancreas, a lipase, digests the fat.
About seven hours after you have eaten your food, it passes from the duodenum into the small intestine where most of the nutrients liberated by the enzymes are absorbed and pass into your blood.

The work of the enzymes is over. They have performed a small miracle. They have helped to transform food into tiny nutrients that the body can absorb and use to renew ageing cells and to provide energy.

Each day muscles burn up several hundred grains of carbohydrate and fat for energy. Without enzymes, our bodies would cease to function.