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Dna and Rna Essay

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Invertase is a yeast derived enzyme. Invertase splits sucrose into glucose and fructose.

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 beta-fructofuranoside 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.

A wide range of microorganisms produce invertase and can, thus, utilize sucrose as a nutrient.

Commercially, invertase is biosynthesized chiefly by yeast strains of Saccharomyces cerevisiae or Saccharomyces carlsbergensis. Even within the same yeast culture, invertase exists in more than one form. For example, the intracellular invertase has a molecular weight of 135,000 Daltons, whereas the extracellular variety has a molecular weight of 270,000 Daltons.

In contrary to most other enzymes, invertase exhibits relatively high activity over a broad range of pH (3.5--5.5), with the optimum near pH=4.5. The enzyme activity reaches a maximum at about 55ÂșC. The Michaelis-Menten values of various enzymes vary widely, but for most enzymes Km is between 2 mM and 5 mM. The Michaelis-Menten value for the free enzyme is typically approx. 30 mM.

Enzyme inhibition is an extremely important area of research in the medical field. For example, lead, mercury, other heavy metals, and nerve gases...

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