Recombinant bacterial phytases and uses thereof

Food or edible material: processes – compositions – and products – Products per se – or processes of preparing or treating... – Protein – amino acid – or yeast containing

Reexamination Certificate

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C435S018000, C435S196000, C435S252300, C435S195000, C435S320100, C536S023200, C530S350000

Reexamination Certificate

active

06855365

ABSTRACT:
A purified and modified phytase enzyme fromEscherichia coliK12 appA phytase is provided. The enzyme has phytase activity and improved thermal tolerance as compared with the wild-type enzyme. In addition, the enzyme has improved protease stability at low pH. Glycosylation of the modified phytase provided a further improved enzyme having improved thermal tolerance and protease stability. The enzyme can be produced from native or recombinant host cells and can be used to aid in the digestion of phytate where desired. In particular, the phytase of the present invention can be used in foodstuffs to improve the feeding value of phytate rich ingredients.

REFERENCES:
patent: 5284933 (1994-02-01), Döbeli et al.
patent: 5593963 (1997-01-01), Van Ooijen et al.
patent: 0 282 042 (1994-06-01), None
patent: 0 897 985 (1999-02-01), None
patent: 0 897 985 (1999-02-01), None
patent: WO 9908539 (1999-02-01), None
Stephen F. Altschul, Warren Gish, Webb Miller, Eugene W. Myers and David J. Lipman, “Basic Local Alignment Search Tool”, 1990, Academic Press Limited, J. Mol. Bio. vol. 215, pp. 403-410.
Henrik Brinch-Pedersen, Annette Olesen, Soren K. Rasmussen & Preben B. Holm, “Generation of Transgenic Wheat (Triticum aestivumL.) for Constitutive Accumulation of an Aspergillus Phytase”, 2000, Molecular Breeding, pp. 195-206.
Janie Dassa, Christian Marck, and Paul L. Boquet, “The Complete Nucleotide Sequence of theEscherichia coliGene appA Reveals Significant Homology between pH 2.5 Acid Phosphatase and Glucose-1-Phosphatase”, Sep., 1990, Journal of Bacteriology, vol. 172, No. 9, pp. 5497-5500.
J. Dvorakova, “Phytase: Sources, Preparation and Exploitation”, 1998, Folia Microbiol, vol. 43(4), pp. 323-338.
Lori Giver, Anne Gershenson, Per-Ola Freskgard, and Frances H. Arnold, “Directed Evolution of a Thermostable Esterase”, Oct., 1998, National Academy of Sciences, vol. 95, pp. 12809-12813.
R. Greiner, U. Konietzny, and Kl..-D. Jany, “Purification and Characterization of Two Phytases fromEscherichia coli”, May 15, 1993, Archives of Biochemistry and Biophysics, vol. 303, No. 1, pp. 107-113.
M. Lehmann, L. Pasamontes, s. F. Lassen, M. Wyss, “The Consensus Concept for Thermostability Engineering of Proteins”,2000, Biochimica et Biophysica Acta, vol. 1543, pp. 408-415.
Lutz Jermutus, Michel Tessier, Luis Pasamontes, Adolphus P.G.M. van Loon, and Martin Lehmann, “Structure-based Chimeric Enzymes as an Alternative to Directed Enzyme Evolution: Phytase as a Test Case”, 2001, Journal of Biotechnology vol. 85, pp. 15-24.
William R. Pearson and David J. Lipman, “Improved Tools for Biological Sequence Comparison”, Apr. 1988, National Academy of Sciences, vol. 85, pp. 2444-2448.
Jan Pen, Theo C. Verwoerd, Peter A. vanParidon, Rob F. Beudeker, Peter J.M. van den Elzen, Kees Geerse, Jan D. van der Klis, Hans A. J. Versteegh, Albert J.J. van Ooyen and Andre′ Hoekema, “Phytase-containing Transgenic Seeds as a Novel Feed Additive for Improved Phosphorus Utilization”, Jul., 1993, Bio/Technology vol. 11, pp. 79-82.
Eric Rodriguez, Yanming Han, and Xin Gen Lei, “Cloning, Sequencing, and Expression of anEscherichia coliAcid Phosphatase/Phytase Gene (appA2) Isolated from Pig Colon”, 1999, Biochemical and Biophysical Research Communications, vol. 257, pp. 117-123.
J. Rozas and R. Rozas, “DnaSP, DNA Sequence Polymorphism: An Interactive Program for Estimating Population Genetics Parameters from DNA Sequence Data”, 1995, Cabios, vol. 11 No. 6, pp. 61-625.
Andrea Tomschy, Michel Tessier, Markus Wyss, Roland Brugger, Clemens Broger, Line Schnoebelen, Adolphus P.G.M. van Loon, and Luis Pasamontes, “Optimizaton of the Catalytic Properties ofAspergillus-fumigatusPhytase Based on the Three-dimensional Structure”, 2000, Protein Science, pp. 1304-1311, vol. 9.
T.C. Verwoerd, A. Hoekema, P. A. van Paridon, A.J.J. van Ooyen, & J. Pen, “Phytase-enriched Transgenic Seeds as a Novel Feed Additive”, 1993, Med. Fac. Landbouww. Univ. Gent. No. 58/4a, pp. 1719-1721.
Costantino Vetriani, Dennis L. Maeder, Nicola tolliday, Kitty S.-P. Yip, Timothy J. Stillman, K. Linda Britton, David W. Rice, Horst H. Klump, and Frank T. Robb, “Protein Thermostability Above 100° C: A Key Role for Ionic Interactions”, Oct., 1998, National Academy of Sciences, vol. 95, pp. 12300-12305.
Gunnar von Heijne, A New Method for Predicting Signal Sequence Cleavage Sites, 1986, Research Group for Theoretical Biophysics, pp. 4683-4690.
Markus Wyss, Roland Brugger, Alexandra Kronenberger, Roland Remy, Rachel Fimbel, Gottfried Oesterhelt, Martin Lehmann, and Adolphus P.G.M. van Loon, Feb., 1999, Applied and Environmental Microbiology, vol. 65, No. 2, pp. 367-373.
Database accession No. AR130956, 2001.
Database accession No. AAX26540.
Database accession No. P07102, 2002.
Arnold, “Enzyme engineering reaches the boiling point”,Proc. Natl. Acad. Sci. USA, vol. 95, pp. 2035-2036, Mar. 1998.
M. Lehmann et al., “Exchanging the active site between phytases for altering the functional properties of the enzyme,”Protein Science, pp. 1866-1872, 2000.
M. Lehmann et al., “From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase”,Protein Engineering, vol. 13, No. 1, pp. 49-57, 2000.
E. Rodriguez et al., Site-Directed Mutagenesis Improves Catalytic Efficiency and Thermostability ofEscherichia colipH 2.5 Acid Phosphatase/Phytase Expressed inPichia pastoris, Archives of Biochemistry and Biophysics, vol. 382, No. 1, Oct. 1, 2000, pp. 105-112.
Altschul et al., “Basic Local Alignment Search Tool,”J. Mol. Biol.215:403-410 (1990).
Dassa et al., “The Complete Nucleotide Sequence of theEscherichia coliGene appA Reveals Significant Homology between pH 2.5 Acid Phosphatase and Glucose-1-Phosphatase,”Journal of Bacteriology172(9):5497-5500 (1990).
Pearson and Lipman, “Improved tools for biological sequence comparison,”Proc. Natl. Acad. Sci. USA85:2442-2448 (1988).
Pen et al., “Phytase-containing Transgenic Seeds as a Novel Feed Additive for Improved Phosphorus Utilization,”Bio/Technology11(7):811-814 (1993).
Rodriguez et al., “Cloning, Sequencing, and Expression of anEscherichia coliAcid Phosphatase/Phytase Gene (appA2) Isolated from Pig Colon,”Biochemical and Biophysical Research Communications257:117-123 (1999).
J. Rozas and R. Rozas, “DnaSP, DNA sequence polymorphism: an interactive program for estimating population genetics parameters from DNA sequence data,”CABIOS11(6):621-625 (1995).
Verwoerd et al., “Phytase-Enriched Transgenic Seeds as a Novel Feed Additive,”Med. Fac. Landbouww. Univ. Gent.,58(4A):1719-1721 (1993).
G. von Heijne, “A new method for predicting signal sequence cleavage sites,”Nucleic Acids Research14(11):4683-4690 (1986).
Database accession No. AAX26540, 2000.
Broun, et al., “Catalytic Plasticity of Fatty Acid Modification Enzymes Underlying Chemical Diversity of Plant Lipids”,Science, vol. 282, pp. 1315-1317, Nov. 13, 1998.
Van de Loo, et al., “An oleate 12-hydroxylase fromRicinus communisL. is a fatty acyl desaturase homolog”,Proc. Natl. Acad. Sci.,vol. 2, pp. 6743-6747, 1995.
Seffernick, et al., “Melamine Deaminase and Atrazine Chlorohydrolase: 98 percent Identical but Functionally Different”,Journal of Bacteriology, vol. 183, No. 8; pp. 2405-1410, Apr., 2001.
Bork, “Powers and Pitfalls in Sequence Analysis: The 70% Hurdle”,Genome Research, vol. 10, pp. 398-400, 2000.
Golovan et al., Characterization and overproduction of theEscherichia coli appAencoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities,Canadian Journal of Microbiology, vol. 46, No. 1, pp. 59-71, Jan., 2000.
Database accession No. A02249, 1996.

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