Phytase expression systems and methods of making and using them
Patent 7232677 Issued on June 19, 2007. Estimated Expiration Date: February 5, 2021. Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.
435/196, Acting on ester bond (3.1)435/320.1, VECTOR, PER SE (E.G., PLASMID, HYBRID PLASMID, COSMID, VIRAL VECTOR, BACTERIOPHAGE VECTOR, ETC.) BACTERIOPHAGE VECTOR, ETC.)435/69.1, Recombinant DNA technique included in method of making a protein or polypeptide435/19, Involving esterase435/252.3, Transformants (e.g., recombinant DNA or vector or foreign or exogenous gene containing, fused bacteria, etc.)435/325, ANIMAL CELL, PER SE (E.G., CELL LINES, ETC.); COMPOSITION THEREOF; PROCESS OF PROPAGATING, MAINTAINING OR PRESERVING AN ANIMAL CELL OR COMPOSITION THEREOF; PROCESS OF ISOLATING OR SEPARATING AN ANIMAL CELL OR COMPOSITION THEREOF; PROCESS OF PREPARING A COMPOSITION CONTAINING AN ANIMAL CELL; CULTURE MEDIA THEREFORE435/410, PLANT CELL OR CELL LINE, PER SE (E.G., TRANSGENIC, MUTANT, ETC.); COMPOSITION THEREOF; PROCESS OF PROPAGATING, MAINTAINING, OR PRESERVING PLANT CELL OR CELL LINE; PROCESS OF ISOLATING OR SEPARATING A PLANT CELL OR CELL LINE; PROCESS OF REGENERATING PLANT CELLS INTO TISSUE, PLANT PART, OR PLANT, PER SE, WHERE NO GENOTYPIC CHANGE OCCURS; MEDIUM THEREFORE435/411, Tomato cell or cell line, per se435/412, Corn cell or cell line, per se435/414, Tobacco cell or cell line, per se435/415, Soybean cell or cell line, per se435/416, Sunflower cell or cell line, per se435/417, Potato cell or cell line, per se435/21, Involving phosphatase435/195, Hydrolase (3. )536/23.2, Encodes an enzyme536/23.7, Encodes a microbial polypeptide530/350, PROTEINS, I.E., MORE THAN 100 AMINO ACID RESIDUES424/442Animal food
The invention provides a purified or recombinant phytase enzyme (SEQ ID NO:2) initially derived from Escherichia coli B. The enzyme has a molecular weight of about 47.1 kilodaltons and has phytase activity (SEQ ID NO:2). 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.
Other References
Casey et al. , J. Biotechnology 110(3):313-322, 2004.
Guo et al., PNAS 101(25):9205-9210, 2004.
Kappel et al., Current Opinion in Biotechnology 3:548-553, 1992.
Mullins et al., Hypertension 22(4):630-633, 1993.
Mullins et al., J. Clin. Invest. 97(7):1557-1560, 1996.
Wigley et al., Reprod. Fert. Dev. 6:585-588, 1994.
Seffernick et al., J. Bacteriol. 183(8):2405-2410, 2001.
Branden et al., Introduction to Protein Structure, Garland Publishing Inc., New York, p. 247, 1991.
Altschul et al., “Basic Local Alignment Search Tool,” J. Mol. Biol. 215:403-410 (1990).
Dassa et al., “The Complete Nucleotide Sequence of the Escherichia coli Gene appA Reveals Significant Homology between pH 2.5 Acid Phosphatase and Glucose-1-Phosphatase,” Journal of Bacteriology 172(9):5497-5500 (1990).
Pearson and Lipman, “Improved tools for biological sequence comparison,” Proc. Natl. Acad. Sci. USA 85:2442-2448 (1988).
Pen et al., “Phytase-containing Transgenic Seeds as a Novel Feed Additive for Improved Phosphorus Utilization,” Bio/Technology 11(7):811-814 (1993).
Rodriguez et al., “Cloning, Sequencing, and Expression of an Escherichia coli Acid Phosphatase/Phytase Gene (appA2) Isolated from Pig Colon,” Biochemical and Biophysical Research Communications 257:117-123 (1999).
J. Rozas and R. Rozas, “DnaSP, DNA sequence polymorphism: an interactive program for estimating population genetics parameters from DNA sequence data,” CABIOS 11(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 Research 14(11):4683-4690 (1986).
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 aestivum L.) 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 the Escherichia coli Gene 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 from Escherichia 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 an Escherichia coli Acid 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, “Optimization of the Catalytic Properties of Aspergillus-fumigatus Phytase Based on the Three-dimensional Structure”, 2000, Protein Science, pp. 1304-1311.
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, Feb. 2001.
Database accession No. AAX26540, May 1999.
Database accession No. P07102, 1990.
Database accession No. A02249, Apr. 1996.
Golovan et al., Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities, Canadian Journal of Microbiology, vol. 46, No. 1, pp. 59-71, Jan. 2000.
Bae et al., Geneseq accession No. ABK12514, Dec. 15, 1999.
Forsberg et al., Geneseq accession No. AAC68296, Nov. 2, 2000.
Forsberg et al., Geneseq accession No. AAC68299, Nov. 2, 2000.
International Search Report, for PCT patent application No. PCT/US02/16482 filed on May 24, 2002.
Ostanin et al., GenBank accession No. L03371 (1992).
Ostanin et al., J Biol Chem 267(32):22830-22836 (1992).
Berka et al., Applied and Environ. Biol. (1998) 64:4423-4427.
Boquet et al., J. of Bacteriology (1987) 169:1663-1669.
Delagrave et al., Protein Eng. (1993) 6:327-331.
Delagrave et al., Nature Biotech. (1993) 11:1548-1552.
Greiner et al., Archives of Biochemistry and Biophysics (1997) 341:201-206.
Institute of Applied Environmental Economics (TME) of the Netherlands, “Use of Phytase in Pig and Poultry Feed to Reduce Phosphorus Excretion,” (1995).
Kerovuo et al., Applied and Environ. Biol. (1998) 64:2079-2085.
Lim et al., Nature Structural Biology (2000) 7:108-113.
NCBI GenBank entry AAB96873 phytase.
NCBI GenBank entry AAA16898 phytase.
NCBI GenBank entry AAB26466 phytase.
NCBI GenBank entry AAB96871 phytase.
OH et al., Abstracts of the General Meeting of the American Society for Microbiology (2000) 100:499-500.
Rodriguez et al., Archives of Biochemistry and Biophysics (1999) 365:262-267.
Rodriguez et al., Archives of Biochemistry and Biophysics (2000) 382:105-112.
Van Hartingsveldt et al., Gene (1993) 127:87-94.
Witkowski et al., Biochemistry (1999) 38:11643-11650.
Wodzinski and Ullah, “Phytase,” in Advantages in Applied Microbiology, Academic Press Inc., vol. 42, (1996) pp. 263-302.
European Search Report for EP 05 01 3009, mailed on Oct. 7, 2005, 4 pages.
Branden et al., Introduction to Protein Science, Garland Publishing Inc., New York, (1991) p. 247.
Supplementary Partial European Search Report for EP 02 74 4174, mailed on Apr. 4, 2006, 7 pages.
February 5, 2021. Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.
