Hafnia phytase
AssigneeNovozymes A/S
InventorsSoeren Flensted Lassen, Carsten Sjoeholm, Lars Kobberoee Skov
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AssigneeNovozymes A/S
InventorsSoeren Flensted Lassen, Carsten Sjoeholm, Lars Kobberoee Skov
Estimating the term…
The present invention relates to isolated polypeptides having phytase activity and isolated polynucleotides encoding the polypeptides. The polypeptides are related to a phytase derived from Hafnia alvei, the amino acid sequence of which is shown in the appended sequence listing as SEQ ID NO: 10. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods for producing and using the polypeptides, in particular within animal feed.
An isolated polypeptide having phytase activity selected from the group consisting of:
Dependencies are inferred from the claim text.
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Hydrolases: acting on ester bonds
Amino acids; Derivatives thereof: polymeric derivatives, e.g. peptides or proteins
Organic substances: vitamins
Organic substances: enzymes
About 2 years 7 months of term left · ends 26 May 2029 (estimated)
Sequence Listing
The present application contains a computer readable form of a sequence listing. The contents of the computer readable form are fully incorporated herein by reference.
Deposit of Biological Material
FIG. 1 shows the residual inositol-phosphate bound phosphorous after in vitro incubation in a comparison between the Hafnia alvei phytase and a Citrobacter braakii phytase dosed from 125 to 500 FYT/kg Feed.
FIG. 2 shows a comparison of the residual inositol-phosphate bound phosphorous after in vitro incubation between the Hafnia alvei phytase and a Peniophora lycii phytase dosed at 250 FYT/kg Feed and 500 FYT/kg Feed.
FIG. 3 shows the Appendix of the structural coordinates for the solved crystal three dimensional structure of the Hafnia alvei phytase.
Phytase activity: In the present context a polypeptide having phytase activity (a phytase) is an enzyme which catalyzes the hydrolysis of phytate (myo-inositol hexakis-phosphate) to (1) myo-inositol and/or (2) mono-, di-, tri-, tetra- and/or penta-phosphates thereof and (3) inorganic phosphate.
The ENZYME site at the internet (www.expasy.ch/enzyme/) is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUB-MB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided (Bairoch A. The ENZYME database, 2000, Nucleic Acids Res 28:304-305). See also the handbook Enzyme Nomenclature from NC-IUBMB, 1992).
According to the ENZYME site, three different types of phytases are known: A 3-phytase (myo-inositol hexaphosphate 3-phosphohydrolase, EC 3.1.3.8), a 6-phytase (myo-inositol hexaphosphate 6-phosphohydrolase, EC 3.1.3.26), and a 5-phytase (EC 3.1.3.72). For the purposes of the present invention, all types are included in the definition of phytase.