Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Patent
1995-05-24
1998-11-10
Grimes, Eric
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
4352523, 43525231, 43525233, 4352543, 4352545, 4352546, 4352549, 43525411, 435325, 426635, C12N 115, C12N 121, C12N 916, C12S 300
Patent
active
058342869
DESCRIPTION:
BRIEF SUMMARY
FIELD OF THE INVENTION
This invention is related to strains of filamentous fungi capable of over-expressing at least two phytate degrading enzymes in desired ratios. Also disclosed are DNA sequences, promoters, DNA constructs and vectors useful for the preparation of such strains.
BACKGROUND OF THE INVENTION
Minerals are essential elements for the growth of all organisms. For livestock production of monogastric animals (e.g., pigs, poultry) and fish, feed is commonly supplemented with minerals. Plant seeds are a rich source of minerals since they contain ions that are complexed with the phosphate groups of phytic acid. Ruminants do not require inorganic phosphate and minerals because microorganisms in the rumen produce enzymes that catalyze conversion of phytate (myo-inositol-hexaphosphate) to inositol and inorganic phosphate. In the process minerals that have been complexed with phytate are released.
Phytate occurs as a source of stored phosphorus in virtually all plant feeds (for a review see: Phytic Acid, Chemistry and Applications, E. Graf (Ed.), Pilatus Press: Minneapolis, Minn., U.S.A., 1986). Phytic acid forms a normal part of the seed in cereals and legumes. It functions to bind dietary minerals that are essential to the new plant as it emerges from the seed. When the phosphate groups of phytic acid are removed by the seed enzyme phytase, the ability to bind metal ions is lost and the minerals become available to the plant. In livestock feed grains, the trace minerals bound by phytic acid are only partially available for absorption by monogastric animals, which lack phytase activity. Although some hydrolysis of phytate occurs in the colon, most phytate passes through the gastrointestinal tract of monogastric animals and is excreted in the manure contributing to fecal phosphate pollution problems in areas of intense livestock production. Inorganic phosphorus released in the colon has no nutritional value to livestock because inorganic phosphorus is absorbed only in the small intestine. Thus, a significant amount of the nutritionally important dietary minerals are potentially not available to monogastric animals.
Conversion of phytate to inositol and inorganic phosphorus can be catalyzed by microbial enzymes referred to broadly as phytases. Phytases such as the phytase #EC 3.1.3.8 are capable of catalyzing hydrolysis of myo-Inositol hexaphosphate to D-myo-inositol 1,2,4,5,6-pentaphosphate and orthophosphate. Certain fungal phytases reportedly hydrolyze inositol pentaphosphate to tetra-, tri-, and lower phosphates; e.g., A. ficuum phytases reportedly produce mixtures of myoinositol di- and mono-phosphate (Ullah, 1988). Phytase producing microorganisms comprise bacteria such as Bacillus subtilis (V. K. Powar and V. J. Jagannathan, J. Bacteriol. 151:1102-1108, 1982) and Pseudomonas (D. J. Cosgrove, Austral. J. Biol. Sci. 23:1207-1220, 1970); yeasts such as Saccharomyces cerevisiae (N. R. Nayini and P. Markakis, Lebensmittel Wissenschaft und Technologie 17:24-26, 1984); and fungi such as Aspergillus terreus (K. Yamada, Y. Minoda and S. Yamamoto, Agric. Biol. Chem. 32:1275-1282, 1968). The possible use of microbes capable of producing phytase as a feed additive for monogastric animals has been reported previously (Shieh and Ware, U.S. Pat. No. 3,297,548; Nelson, T. S. et al., J. Nutrition 101:1289-1294, 1971). To date, however, commercial application of this concept has not proved feasible, because of the high cost for production of microbial phytases.
Microbial phytases may also reportedly be useful for producing animal feed from certain industrial processes, e.g., wheat and corn waste products. The wet milling process of corn produces glutens sold as animal feeds. Addition of phytase may reportedly improve the nutritional value of the feed product. Fungal phytase enzymes and process conditions (t.about.50.degree. C. and pH.about.5.5) have been reported previously in European Patent Application 0 321 004. In processing soybean meal the presence of phytate reportedly renders the meal and wastes unsuit
REFERENCES:
patent: 3297548 (1967-01-01), Ware et al.
patent: 3966971 (1976-06-01), Morehouse et al.
patent: 4914029 (1990-04-01), Caransa et al.
patent: 5217959 (1993-06-01), Sabin
patent: 5298405 (1994-03-01), Nevalainen et al.
patent: 5436156 (1995-07-01), Van Gorcom et al.
patent: 5443979 (1995-08-01), Vanderbeke et al.
patent: 5554399 (1996-09-01), Vanderbeke et al.
patent: 5593963 (1997-01-01), Van Ooijen et al
MacRae et al., 71:339-348, 1988.
Bailey, M.J. and K.M.H. Nevalainen, "Induction, isolation and testing of stable Trichoderma reesei mutants with improved production of solubilizing cellulase," Enzyme Microb. Technol. 3:153-157 (1981).
Ehrlich, K.C. et al., "Identification and cloning of a second phytase gene (phyB) from Aspergillus niger (ficuum)," Biochem. Biophys. Res. Comm. 195(1):53-57 (Aug. 1993).
Fujiwara, S. et al., "Hydrolysis of phytate in soybean by phytase from Rhizopus sp. EF-78," Chem. Abstr. 106:266, Abstract No. 115629m (1987).
Gibson, D.M., "Production of Extracellular Phytase from Aspergillus ficuum on Starch Media," Biotechnol. Letts. 9(5):305-310 (1987).
Gibson, D.M. and A.B.J. Ullah, "Phytases and Their Action on Phytic Acid," Inositol Metabolism in Plants, Moore, D.J. et al., eds., Wiley-Liss, New York, publ., pp. 77-92 (1990).
Houston, C.S. et al., "The Cloning and Overexpression of Phytase and pH 2.5 Acid Phosphatase in Aspergillus niger: Applications to a Commercial Product," presented at Society for Industrial Microbiology annual meeting, San Diego, CA, Aug. 9-14, 1992.
Innis, M.A. et al., "Expression, Glycosylation, and Secretion of an Aspergillus Glucoamylase by Saccharomyces cerevisiae," Science 288:21-26 (Apr. 1985).
"Microbial Phytase to be Used in Food Processing," European Biotechnology Newsletter 75:05 (Sep. 1989).
Nayini, N.R. and P. Markakis, "The Phytase of Yeast," Lebensm.-Wiss. u. -Technol. 17: 24-26 (1984).
Ohtsuka, E. et al., "An Alternative Approach to Deoxyoligonucleotides as Hybridization Probes by Insertion of Deoxyinosine at Ambiguous Codon Positions," J. Biol. Chem. 260(5):2605-2608 (Mar. 1985).
Penttila, M. et al., "A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei," Gene 61: 155-164 (1987).
Powar, V.K. and V. Jagannathan, "Purification and Properties of Phytate-Specific Phosphatase from Bacillus subtilis," J. Bacteriol. 151(3):1102-1108 (Sep. 1982).
Saloheimo, M. and M.-L. Niku-Paavola, "Heterologous Production of a Ligninolytic Enzyme: Expression of the Phlebia radiata Laccase Gene in Trichoderma reesei," Bio/Technol. 9:987-990 (Oct. 1991).
Ullah, A.H.J. and B.J. Cummins, "Aspergillus ficuum Extracellular pH 6.0 Optimum Acid Phosphatase: Purification, N-Terminal Amino Acid Sequence, and Biochemical Characterization," Prep. Biochem. 18(1):37-65 (1988).
Ullah, A.H.J. and H.C. Dischinger, Jr., "Aspergillus ficuum Extracellular Phytase: Peptide Mapping and Purification by Reverse Phase Chromatography," Ann. New York Acad. Sci. 613:878-882 (Dec. 1990).
Ullah, A.H.J. and C. Dischinger, "Identification of active-site residues in Aspergillus ficuum extracellular pH 2.5 optimum acid phosphatase," Biochem. Biophys. Res. Comm. 192:754-759 (1993).
van Hartingsveldt, W. et al., "Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger," Gene 127:87-94 (May 1993).
Yamada, K. et al., "Phytase from Aspergillus terreus: Part I. Production, Purification and Some General Properties of the Enzyme," Agr. Biol. Chem. 32(10): 1275-1282 (1968).
Yamamoto, S. et al., "Chemical and Physicochemical Properties of Phytase from Aspergillus terreus," Agr. Biol. Chem. 36(12):2097-2103 (1972).
Dialog File 16, "Strategic Partners Report," Genetic Technology News (Oct. 1991).
Dialog File 583, "Collaborative research gains bio-technology break through," International Milling Flour & Feed (IMFF), Infomat No. 04630360, p. 6 (Oct. 1991).
Arima, K., et al., "The Nucleotide Sequence of the Yeast PH05 Gene: A Putative Precursor of Repressible Acid Pho
Cantrell Michael A.
Fagerstrom Richard B.
Houston Christine S.
Miettinen-Oinonen Arja S. K.
Nevalainen Helena K. M.
Grimes Eric
Rohm Enzyme Finland Oy
LandOfFree
Recombinant cells that express phytate degrading enzymes in desi does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Recombinant cells that express phytate degrading enzymes in desi, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Recombinant cells that express phytate degrading enzymes in desi will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-1515774