An Enzyme, any one of many specialised organic substances, composed of polymers of amino acids, that act as catalysts to regulate the speed of the many chemical reactions involved in the metabolism of living organisms. The name enzyme was suggested in 1867 by the German physiologist Wilhelm Kühne (1837-1900); it is derived from the Greek phrase enzyme, meaning in leaven.  Those enzymes identified now number well over 700. Enzymes are classified into several broad categories, such as hydrolytic, oxidising, and reducing, depending on the type of reaction they control. Hydrolytic enzymes accelerate reactions in which a substance is broken down into simpler compounds through reaction with water molecules. Oxidising enzymes, known as oxidases, accelerate oxidation reactions; reducing enzymes speed up reduction reactions, in which oxygen is removed. Many other enzymes catalyse other types of reactions. Individual enzymes are named by adding ase to the name of the substrate with which they react. The enzyme that controls urea decomposition is called urease; those that control protein hydrolyses are known as proteinases. Some enzymes, such as the proteinases trypsin and pepsin, retain the names used before this nomenclature was adopted. Properties of Enzymes As the Swedish chemist Jöns Jakob Berzelius suggested in 1823, enzymes are typical catalysts: they are capable of increasing the rate of reaction without being consumed in the process. See CATALYSIS below. Some enzymes, such as pepsin and trypsin, which bring about the digestion of meat, control many different reactions, whereas others, such as urease, are extremely specific and may accelerate only one reaction. Still others release energy to make the heart beat and the lungs expand and contract. Many facilitate the conversion of sugar and foods into the various substances the body requires for tissue-building, the replacement of blood cells, and the release of chemical energy to move muscles. Pepsin, trypsin, and some other enzymes possess, in addition, the  peculiar property known as autocatalysis, which permits them to  cause their own formation from an inert precursor called zymogen.  As a consequence, these enzymes may be reproduced in a test  tube.  As a class, enzymes are extraordinarily efficient. Minute  quantities of an enzyme can accomplish at low temperatures what  would require violent reagents and high temperatures by ordinary  chemical means. About 30 g (about 1 oz) of pure crystalline  pepsin, for example, would be capable of digesting nearly 2  metric tons of egg white in a few hours. The kinetics of enzyme reactions differ somewhat from those of simple inorganic reactions. Each enzyme is selectively specific  for the substance in which it causes a reaction and is most  effective at a temperature peculiar to it. Although an increase in  temperature may accelerate a reaction, enzymes can be unstable  when over heated. The catalytic activity of an enzyme is  determined primarily by the enzyme's amino-acid sequence and  by the tertiary structure that is, the three-dimensional folded structure of the macromolecule. Many enzymes require the presence of another ion or a molecule, called a cofactor, in order to function.  As a rule, enzymes do not attack living cells. As soon as a cell dies, however, it is rapidly digested by enzymes that break down protein.  The resistance of the living cell is due to the enzyme's inability to pass through the membrane of the cell as long as the cell lives. When the cell dies, its membrane becomes permeable, and the enzyme can then enter the cell and destroy the protein within it. Some cells also contain enzyme inhibitors, known as antienzymes, which prevent the action of an enzyme upon a substrate.
 

Practical Uses of Enzymes
Alcoholic fermentation and other important industrial processes depend on the action of enzymes that are synthesised by the yeasts and bacteria used in the production process. A number of enzymes are used for medical purposes. Some have been useful in treating areas of local inflammation; trypsin is employed in removing foreign matter and dead tissue from wounds and burns.

Historical Review
Alcoholic fermentation is undoubtedly the oldest known enzyme reaction. This and similar phenomena were believed to be spontaneous reactions until 1857, when the French chemist Louis Pasteur proved that fermentation occurs only in the presence of living cells. Subsequently, however, the German chemist Eduard Buchner discovered (1897) that a cell-free extract of yeast can cause alcoholic fermentation.  The ancient puzzle was then solved; the yeast cell produces the enzyme, and the enzyme brings about the fermentation. As early as 1783 the Italian biologist Lazzaro Spallanzani had observed that meat could be digested by gastric juices extracted from hawks. This experiment was probably the first in which a vital reaction was performed outside the living organism. After Buchner's discovery scientists assumed that fermentations and vital reactions in general were caused by enzymes. Nevertheless, all attempts to isolate and identify their chemical nature were unsuccessful. In 1926, however, the American biochemist James B. Sumner succeeded in isolating and crystallising urease. Four years later pepsin and trypsin were isolated and crystallised by the American biochemist John H. Northrop. Enzymes were found to be proteins and Northrop proved that the protein was actually the enzyme and not simply a carrier for another compound.  Research in enzyme chemistry in recent years has shed new light on some of the most basic functions of life. Ribonuclease, a simple three-dimensional enzyme discovered in 1938 by the American bacteriologist René Dubos and isolated in 1946 by the
American chemist Moses Kunitz, was synthesised by American researchers in 1969. The synthesis involves hooking together 124 molecules in a very specific sequence to form the macromolecule. Such syntheses led to the probability of identifying those areas of the molecule that carry out its chemical functions, and opened up the possibility of creating specialised enzymes with properties not possessed by the natural substances. This potential has been greatly expanded in recent years by genetic engineering techniques that have made it possible to produce some enzymes in great quantity. The medical uses of enzymes are illustrated by research into L-asparaginase, which is thought to be a potent weapon for treatment of leukaemia; into dextrinases, which may prevent tooth decay; and into the malfunctions of enzymes that may be linked to such diseases as phenylketonuria, diabetes, and  anaemia and other blood disorders.

CATALYST
Catalysis, alteration of the speed of a chemical reaction, through the presence of an additional substance, known as a catalyst, that remains chemically unchanged by the reaction. Enzymes, which are among the most powerful catalysts, play an essential role in living organisms, where they accelerate reactions that otherwise would require temperatures that would destroy most of the organic matter. A catalyst in a solution with or in the same phase as the reactants is called a homogeneous catalyst. The catalyst combines with one of the reactants to form an intermediate compound that reacts more readily with the other reactant. The catalyst, however, does not influence the equilibrium of the reaction, because the decomposition of the products into the reactants is speeded up to a similar degree.  An example of homogeneous catalysis is the formation of sulfur trioxide by the reaction of sulfur dioxide with oxygen, in which nitric oxide serves as a catalyst. The reaction temporarily forms the intermediate compound nitrogen dioxide, which then reacts with oxygen to form sulfur oxide. The same amount of nitric oxide exists at the end as at the start of the reaction.  A catalyst that is in a separate phase from the reactants is said to be a heterogeneous, or contact, catalyst. Contact catalysts are materials with the capability of adsorbing molecules of gases or liquids onto their surfaces. An example of heterogeneous catalysis is the use of finely divided platinum to catalyse the reaction of carbon monoxide with oxygen to form carbon dioxide. This reaction is used in catalytic converters mounted in automobiles to eliminate carbon monoxide from the exhaust gases.  Some substances, called promoters, do not have catalytic ability by themselves but increase the effectiveness of a catalyst. For example, if alumina is added to finely divided iron, it increases the ability of the iron to catalyse the formation of ammonia from a mixture of nitrogen and hydrogen.
Materials that reduce the effectiveness of a catalyst, on the other hand, are referred to as poisons. Lead compounds reduce the ability of platinum to act as a catalyst; therefore, an automobile equipped with a catalytic converter for emission control must be fuelled with unleaded petrol.  Catalysts are of major importance in today's industrial world. It has been estimated that about 20%  of the U.S.A. gross national product is generated through the use of catalytic processes. One current area of active research in catalysis is that of enzymes. Natural enzymes have long been used by a few industries, but fewer than 30 such enzymes are presently available in industrial amounts. Biotechnologists are seeking ways in which to expand this resource and also to develop semisynthetic enzymes for highly specific tasks. Some tasks under development are mining for coal and gold using Enzymes to do the work.

((See some test results) Click here