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Title

PHYTASES: ENZYMOLOGY, MOLECULAR AND BIOCHEMICAL CHARACTERISTIC AND APPLICATIONS

Pages

 Start Page 13 | End Page 39

Abstract

 Phytases are a special class of phosphatses that catalyze the step-wise release of phosphate from PHYTATE, the principle storage form of phosphate in plant seeds. These enzymes have a wide distribution in plants, microorganisms and in some animal tissues; however, microbial sources are more promising for the production. They are added to ANIMAL FEEDSTUFF to reduce phosphate pollution in the environment, since monogastric animals such as pigs, poultry and fish are unable to metabolize PHYTATE. The first commercial PHYTASE product became available on the market around 20 years ago. Based on biochemical properties and amino acid sequence alignment, PHYTASEs can be categorized into four major classes, histidine acid phosphatase, b-propller PHYTASE, cystein phosphatase and purpule acid phosphatase. In general, PHYTASEs behave like a monomeric enzyme with molecular masses between 40 and 100 kDa. Up to now two main types of PHYTASEs have been identified based on optimal pH for activity; acid PHYTASEs with a pH optimum around 5 and alkaline PHYTASEs with a pH optimum around 8. Most of identified PHYTASEs depending upon the source of origin they have generally pH and temperature optima around 4.5-6 and 45-60oC.Some of PHYTASEs show broad substrate specificity and hydrolyzes metal-free PHYTATE, in contrast some of them exhibit strict substrate specificity for the calcium-phytate. PHYTASEs are different according to the number of released phosphate groups from PHYTATE and in general they have capability to release 3 to 5 phosphate groups. This article reviews enzymology, application and biochemical and catalytic characteristic of microbial PHYTASEs.

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