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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Commodity Utilization Research » Research » Publications at this Location » Publication #194774
Title: PHYTASE: SOURCE, STRUCTURE, AND APPLICATION

Author
item LEI, XIN - CORNELL UNIVERSITY
item PORRES, JESUS - UNIVERSITY DE GRANADA
item Mullaney, Edward
item BRINCH-PEDERSEN, HENRIK - DANISH INSTITUTE OF AG

Submitted to: Book Chapter
Publication Type: Book / Chapter
Publication Acceptance Date: 12/31/2005
Publication Date: 5/1/2007
Citation: Lei, X. G., Porres, J. M., Mullaney, E. J. and Brinch-Pedersen, H. 2007. Phytase: source, structure and application. In: Industrial Enzymes, structure, function and applications. Editied by Polina, J. and MacCabe, A. P. Springer, Dordrecht, The Netherlands, p. 505-529.

Interpretive Summary: Phytases have been one of the most extensively studied enzymes for nutrition, environmental protection, and human health during the past two decades. These enzymes break down phytic acid, which is found widely in plant grains and seeds. It is the major chemical form of phosphorus in plants. Various phytases have been isolated from plants and microbes, and can be grouped based on their pH optima (alkaline or acid phytases), catalytic mechanisms, or the order in which phosphates groups are liberated. Recent phytase research has been driven by the urgent need for improving utilization of phytate-phosphorus in diets for simple-stomached animals to reduce their manure phosphorus excretion to environment. However, potential applications of phytases may extend to release dietary phytate-bound minerals for human nutrition and to develop special inositol phosphates for human health. This review covers these topics for the major sources of phytase, the structure of the different types of phytate degrading enzymes, and the current and potential future uses of this enzyme.

Technical Abstract: Phytases have been one of the focal enzymes for nutrition, environmental protection, and human health during the past two decades. These enzymes sequentially cleave orthophosphate groups from the inositol core of phytate, the major chemical form of phosphorus in plants. Various phytases have been isolated from plants and microbes, and can be grouped based on their pH optima (alkaline or acid phytases), catalytic mechanisms (histidine acid phosphatases, ß-propeller phytase, cysteine phosphatases or purple acid phosphatases), or stereospecificity of phytate hydrolysis (3- or 6-phytases). Recent phytase research has been driven by the urgent need for improving utilization of phytate-phosphorus in diets for simple-stomached animals to reduce their manure phosphorus excretion to environment. However, potential applications of phytases may extend to release dietary phytate-bound minerals for human nutrition and to develop special inositol phosphates for human health.