Cloning and expression of microbial phytase

Drug – bio-affecting and body treating compositions – Enzyme or coenzyme containing – Hydrolases

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435168, 435196, A61K 3846, C12P 300, C12N 916

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active

058635335

ABSTRACT:
A nucleotide sequence encoding phytase has been isolated and cloned. The coding sequence has been inserted into an expression construct which in turn has been inserted into a vector capable of transforming a microbial expression host. The transformed microbial hosts may be used to economically produce phytase on an industrial scale. The phytase produced via the present invention may be used in a variety of processes requiring the conversion of phytate to inositol and inorganic phosphate.

REFERENCES:
patent: 3297548 (1967-01-01), Ware et al.
Graf, E. ed., Phytic Acid: Chemistry and Applications (1986) Pilatus Press, Minneapolis, MN, Chapter 2, pp. 23-42.
Powar et al., "Purification and Properties of Phytate-Specific Phosphatase from Bacillus subtilis" J. Bacteriol. (1982) 151:1102-1108.
Cosgrove, "Inositol Phosphate Phosphatases of Microbiological Origin. Inositol Phosphate Intermediates in the Dephosphorylation of the Hexaphosphates of Myo-Inositol, Scyllo-Inositol, and D-Chiro-Inositol by a Bacterial (Pseudomonas Sp.) Phytase" Aust. J. Biol. Sci. (1970) 23:1207-20.
Nayini et al., "The Phytase of Yeast" Lebensmittel Wissenschaft und Technologie (1984) 17:24-26.
Yamada et al., "Phytase from Aspergillus terreus" Agr. Biol. Chem. (1968) 32(10):1275-1282.
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Ullah, Enzyme and Engineering Conference IX, Oct. 4-8, 1987, Santa Barbara, CA (poster presentation) 2 pages total.
Ullah, "Aspergillus Ficuum Phytase: Partial Primary Structure, Substrate Selectivity, and Kinetic Characterization" Preparatory Biochem. (1988) 18(4):459-471.
Ullah et al., "Extracellular Phytase (E.C. 3.1.3.8) from Aspergillus Ficuum NRRL 3135: Purification and Characterization" Preparative Biochem. (1987) 17(1):63-91.
Mullaney et al., Filamentous Fungi Conference (Apr. 1987) Pacific Grove, CA (poster presentation) 15 pages total.

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