Introduction

Catalase (EC 1.11.1.6), present in the peroxisomes of nearly all aerobic cells, serves to protect the cell from the toxic effects of hydrogen peroxide by catalyzing its decomposition into molecular oxygen and water without the production of free radicals. The mechanism of catalysis is not fully elucidated, but the overall reaction is as follows: 2 H2O2 -- 2 H20 + O2

Hydrogen peroxide (H2O2) is naturally formed in living organisms, however it is very harmful and is broken down immediately by several enzymes including catalase. This enzyme catalyses the breakdown of hydrogen peroxide to water and oxygen. Persons with acatalasemia (a hereditary condition) have extremely low catalase activity and, although present worldwide, it is more commonly found in Koreans.
Catalase was one of the first enzymes to be purified to homogeneity, and has been the subject of intense study. The enzyme is among the most efficient known, with rates approaching 200,000 catalytic events/second/subunit (near the diffusion-controlled limit). Catalase structure from many different species has been studied by X-ray diffraction. Although it is clear that all catalases share a general structure, some differ in the number and identity of domains. In this display, beef liver catalase will be used as a model for catalase structure. It will then be compared to catalase structure from a fungus, Penicillium vitale. The catalase test is used to detect the presence of catalase enzymes by the decomposition of hydrogen peroxide to release oxygen and water. Hydrogen peroxide is formed by some bacteria as an oxidative end product of the aerobic breakdown of sugars. If allowed to accumulate it is highly toxic to bacteria and can result in cell death. Catalase either decomposes hydrogen peroxide or oxidises secondary substrates, but it has no effect on other peroxides3.

Invertase Introduction Our most common food sugarthe disaccharide, sucroseis formed in all green plants. The metabolism of sucrose in the animal body begins with the action of invertase (sucrase) which hydrolyzes the disaccharide to two monosaccharides, fructose and glucose. This same enzyme is also produced by plants and fungi. The official name for invertase is beta-fructofuranosidase (EC3.2.1.26), which implies that the reaction catalyzed by this enzyme is the hydrolysis of the terminal nonreducing betafructofuranoside residues in beta-fructofuranosides. Note that alpha-D-glucosidase, which splits off a terminal glucose unit, can also catalyze this reaction. Note that sucrose can be hydrolyzed relatively easily; the reaction proceeds in an acidic environment without the aid of invertase. Invertase is mainly used in the food (confectionery) industry where fructose is preferred over sucrose because it is sweeter and does not crystallize as easily. However, the use of invertase is rather limited because another enzyme, glucose isomerase, can be used to convert glucose to

fructose more inexpensively. For health and taste reasons, its use in food industry requires that invertase be highly purified.

Invertase (EC 3.2.1.26 ) (systematic name: beta-fructofuranosidase) is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the OC(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond.[1] For industrial use, invertase is usually derived from yeast. It is also synthesized by bees, who use it to make honey from nectar. Optimum temperature at which the rate of reaction is at its greatest is 60 C and an optimum pH of 4.5.[1] Typically, sugar is inverted with sulfuric acid.