Catalysts alter the rates of chemical reactions without being consumed by the reaction.

A catalyst cannot cause a reaction to happen that would not happen anyways, that is, a catalyst cannot influence the free energy change for a reaction. Catalyst speed up reactions by providing alternative faster pathway for reactants to become products. In addition to these general features shared by all catalyst, enzyme has some special properties that make them unique. For one thing, enzyme-catalyzed reactions are very efficient ones with no side reactions. In many of the laboratory reactions we have discussed there are possible side reactions, often resulting in mixtures of products, some of which may not be desired. This wastefulness does not happen in body reactions. But the outstanding future of enzyme activity is that most enzymes are highly specific compared with synthetic catalysts, that is, most enzymes combine with only one substrate or a few closely related substrate. For instance, the only known function of the carbohydrase maltase, is to cut the glicosidic linkage in the distance maltose. No other enzyme can substitute for maltase in this reaction (Solomon, 1987). When enzyme were first discover they were given unsystematic named by their discoverers, such as pepsin, trypsin, ptyalin, etc. In more recent time enzymes have been designated by the suffix -ase preceded by a term which indicates either the general nature of the substrate the actual name of the substrate, the type of reaction catalyzed, or a combination of several of this fact (Cantarow, 1963). An ideal catalyst is a substance which when present in small quantities will alter the rate of a chemical reaction without itself being altered in the process. An ideal catalyst would be expected, therefore, to exert its rate changing effect over indefinite periods of time if sufficient quantities of the reagents concerned are present. Actually, no real catalyst is ideal, and all are, in the course of time as the catalyzed reaction proceeds, rendered inert or poisoned (Boyd, 1957).

The hydrolysis of starch with thermally stable amylase, produced from strain of bacillus subtilis XK-86 carried out with maximum rate at pH 7, concentration of the substrate 250g/l, concentration of the enzyme 12 units per ml suspension and temperature 90C The substrate exert strong inhibiting influence of the enzyme activity at concentration greater than 250 g/l We have established that with the studied enzyme we obtain the high rate of hydrolysis and thus high concentration of reducing sugar in the framework of the relatively short duration 4 hour and 15 min.