Phytases: Microbial Sources, Production, Purification, and Potential Biotechnological Applications

REFERENCES

• Abelson, P. H. 1999. A potential phosphate crisis. Science 283: 2015.
   PubMed Web of Science ®Google Scholar
• Al-Asheh, S. and Duvnjak, Z. 1994. The effect of surfactants on the phytase production and the reduction of the phytic acid content in canola meal by Aspergillus carbonarius during solid-state fermentation process. Biotechnol. Lett. 16(2): 183–188.
   Google Scholar
• Al-Asheh, S. and Duvnjak, Z. 1995. Phytase production and decrease of phytic acid content in canola meal by Aspergillus carbonarius in solid-state fermentation. World J. Microbiol. Biotechnol. 11: 228–231.
   PubMed Web of Science ®Google Scholar
• Amano pharmaceuticals 1995. Novel phytase. Japan Pat. 07 067 635.
   Google Scholar
• Anno, T., Nakanishi, K., Matsuno, R., and Kamikubo, T. 1985. Enzymatic elimination of phytate in soybean milk. J. Japan Soc. Food Sci. Technol. 32: 174–180.
   Google Scholar
• Bali, A. and Satyanarayana, T. 1997. Production and potential application of fungal Phytases. Proceedings of National Symposium on Fungi in Diversified Habitats. Osmania University, Hyderabad. July 12–13 1997, pp. 1–5.
   Google Scholar
• Bali, A. and Satyanarayana, T. 1999. Microbial Phytases in Food Biotechnology. In: Microbial Biotechnology. pp. 93–110. Gupta, R. and Chamola, B. P., Eds., A.P.H Publishing Corporation.
   Google Scholar
• Bali, A. and Satyanarayana, T. 2001. Microbial phytases in nutrition and combating phosphorus pollution. Everyman’s Sci. 4: 207–209.
   Google Scholar
• Berka, R. M., Rey, M. W., Brown, K. M., Byun, T., and Klotz, A. V. 1998. Molecular characterization and expression of a phytase gene from the thermophilic fungus Thermomyces lanuginosus. Appl. Environ. Microbiol. 64: 4423–4427.
   PubMed Web of Science ®Google Scholar
• Berridge, M. J. and Irvine, R. F. 1989. Inositol phosphates and cell signalling. Nature 341: 197–205.
   PubMed Web of Science ®Google Scholar
• Billington, D. C. 1993. The Inositol Phosphates. Chemical Synthesis and Biological Significance. Verlag Chemie, Weinham.
   Google Scholar
• Bitar, K. and Reinhold, J. G. 1972. Phytase and alkaline phosphatase activities in intestinal mucosae of rat, chicken, calf and man. Biochim. Biophys. Acta 268: 442–452.
   PubMed Web of Science ®Google Scholar
• Brocades. 1991a. DNA sequence encoding phytase. Pat. EP 420 358.
   Google Scholar
• Brocades. 1991b. Production of phytase in transgenic plant or plant organ. Pat. EP 449 375.
   Google Scholar
• Caransa, A., Simell, M., Lehmussari, M., Vaara, M., and Vaara, T. 1988. A novel enzyme application in corn wet milling. Starch 40: 409–411.
   Web of Science ®Google Scholar
• Carmovale, E., Lugaro, E., and Lombardi-Boccia, G. 1988. Phytic acid in faba bean and pea: effect on protein availability. Cereal Chem. 65(2): 114–117.
   Google Scholar
• Casida, L. E. Jr. 1959. Phosphatase activity of some common soil fungi. Soil Sci. 87: 305–310.
   Google Scholar
• Chang, C. W. 1967. Study of phytase and fluoride effects in germinating corn seeds. Cereal Chem. 44: 129–142.
   Web of Science ®Google Scholar
• Chen, C., Hunag, C., and Cheng, K. 2001. Improvement of phytase thermostability by using sorghum liquor wastes supplemented with starch. Biotechnol. Lett. 23: 331–333.
   Google Scholar
• Cosgrove, D. J. 1969. Ion exchange chromatography of inositol polyphosphates. Ann. N. Y. Acad. Sci. 165: 677–686.
   Google Scholar
• Cosgrove, D. J. 1970. Inositol phosphates of microbial origin. Inositol phosphate intermediates in the dephosphorylation of the hexaphosphates of myoinositol, scyllo-inositol, and D-chiro-inositol by a bacterial (Pseudomonas sp.) phytase. Austral. J. Biol. Sci. 23: 1207–1220.
   PubMedGoogle Scholar
• Cromwell, G. L., Coffey, R. D., Parker, G. R., Monegue, H. J., and Randolph, J. H. 1995a. Efficacy of low activity microbial phytase in improving the bioavailability of phosphorus in corn-soybean meal diets for pigs. J. Animal Sci. 73: 449–456.
   PubMed Web of Science ®Google Scholar
• Cromwell, G. L., Coffey, R. D., Parker, G. R., Monegue, H. J., and Randolph, J. H. 1995b. Efficacy of a recombinant derived phytase in improving the bioavailability of phosphorus in corn-soybean meal diets for pigs. J. Animal Sci. 73: 2000–2008.
   PubMed Web of Science ®Google Scholar
• Cromwell, G. L., Stahly, T. S., Coffey, R. D., Monegue, H. J., and Randolph, J. H. 1993. Efficacy of phytase in improving the bioavailability of phosphorus in soybean meal and corn-soybean meal diets for pigs. J. Animal Sci. 71: 1831–1840.
   PubMed Web of Science ®Google Scholar
• Dalal, R. C. 1978. Soil organic phosphorus. Adv. Agronom. 29: 83–117.
   Google Scholar
• Dassa, E., Marek, C., and Boquet, P. L. 1990. The complete nucleotide sequence of the E. coli gene app A reveals significant homology between pH 2.5 optimum acid phosphatase and glucose-1-phosphatase. J. Bacteriol. 172: 5497–5500.
   Google Scholar
• Davies, N. T. and Nightingale, R. 1975. The effects of phytate on intestinal absorption and secretion of zinc and whole body retention of zinc, copper, iron and manganese in rats. Br. J. Nutr. 34: 243–258.
   PubMed Web of Science ®Google Scholar
• Day, P. R. 1996. Genetic modification of plants: significant issues and hurdles to success. Am. J. Clin. Nutr. 63: 651S-656S.
   Google Scholar
• De Boland, A. R., Garner, G. B., and O’Dell, B. L. 1975. Identification and properties of “phytate” in cereal grains and oilseed products. J. Agric. Food Chem. 23 : 1186–1189.
   Google Scholar
• Dvorakova, J. 1998. Phytase: Sources, preparation and exploitation. Folia Microbiol. 43(4): 323–338.
   Google Scholar
• Ebune, A., Al-Asheh, S., and Duvnjak, Z. 1995. Effect of phosphate, surfactants and glucose on phytase production and hydrolysis of phytic acid in canola meal by Aspergillus ficuum during solid state fermentation. Biores. Technol. 54: 241–247.
   Web of Science ®Google Scholar
• Ehrlich, K. C., Montalbano, B. G., Mullaney, E. J., Dischinger, H. C., Jr., and Ullah, A. H. J. 1993. Identification and cloning of a second phytase gene (phy B) from Aspergillus niger (ficuum). Biochem. Biophys. Res. Commun. 195: 53–57.
   PubMed Web of Science ®Google Scholar
• Eskin, N. A. M. and Wiebe, S. 1983. Changes in phytate activity and phytase during germination of two fababean cultivars. J. Food Sci. 48: 270–271.
   Web of Science ®Google Scholar
• Fardiaz, D. and Markakis, P. 1981. Degradation of phytic acid in oncom (fermented peanut press cake). J. Food Sci. 46: 523–525.
   Web of Science ®Google Scholar
• Findenegg, G. R. and Nelemans, J. A. 1993. The effect of phytase on the availability of P from myoinositol hexaphosphate (phytate) for maize roots. Plant Soil 154: 189–196.
   Web of Science ®Google Scholar
• Finnish National Public Health Institute. 1994. Grampositive bacterial expression system for enhanced secretion of exoproteins. Pat. WO 9 419 471.
   Google Scholar
• Frolich, W. 1990. Chelating properties of dietary fibre and phytate. The role for mineral availability. Adv. Exp. Med. Biol. 270: 83–93.
   Google Scholar
• Galzy, P. 1964. Etude genetique et physiologique du metabolism de l’acide Lactique chez Saccharomyces cerevisiae. Hansen. Ann. Technol. Agric. 13: 109–259.
   Google Scholar
• Ghareib, M. 1990. Biosynthesis, purification and some properties of extracellular phytase from Aspergillus carneus. Acta. Microbiol. Hung. 37 (2): 159–64.
   Google Scholar
• Ghosh, S. 1997. Phytase of a thermophilic mould Sporotrichum thermophile Apinis. M.Sc dissertation, Department of Microbiology, University of Delhi, Delhi.
   Google Scholar
• Gibson, D. M. 1987. Production of extracellular phytase from Aspergillus ficuum on starch media. Biotechnol. Lett. 5: 305–310.
   Google Scholar
• Gibson, D. M. and Ullah, A. H. J. 1990. Phytases and their action in phytic acid. In: Inositol Metabolism in Plants. pp. 77–92. Wiley-Liss, Chichester.
   Google Scholar
• Golovan, S. P., Hayes, M. A., Phillips, J. P., and Forsberg, C. W. 2001. Transgenic mice expressing bacterial phytase as a model for phosphorus pollution control. Nature Biotech. 19: 429–433.
   PubMed Web of Science ®Google Scholar
• Greaves, M. P., Anderson, G., and Webley, D. M. 1967. The hydrolysis of inositol phosphates by Aerobacter aerogenes. Biochim. Biophys. Acta 132: 412–418.
   Google Scholar
• Greene, D. A., De Jesus, P. V., and Winegrad, A. I. 1975. Effcts of insulin and dietary myoinositol on impaired peripheral motor nerve conduction velocity in acute streptozotocin diabetes. J. Clin. Invest. 55: 1326–1336.
   PubMed Web of Science ®Google Scholar
• Greiner, R., Haller, E., Konietzny, U., and Jany, K. D. 1997. Purification and characterization of phytase from Klebsiella terrigena. Arch. Biochem. Biophys. 341: 201–206.
   PubMed Web of Science ®Google Scholar
• Greiner, R. and Konietzny, U. 1996. Construction of a bioreactor to produce special breakdown products of phytate. J. Biotechnol. 48: 153–159.
   PubMed Web of Science ®Google Scholar
• Greiner, R., Konitzny, U., and Jany, K. D. 1993. Purification and characterization of two phytases from Escherchia coli. Arch. Biochem. Biophys. 303: 107–113.
   PubMed Web of Science ®Google Scholar
• Gutknecht, K. 1997. Green genes: Alfalfa biofarming is about to take root. Wisconsin Agriculturist, Mid-March, pp. 8–10
   Google Scholar
• Ha, N. C., Kim, Y. O., Oh, T. K., and Oh, B. H. 1999. Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain. Acta crystallogr. D. Biol. Crystallogr. 55: 691–693.
   Google Scholar
• Han, Y. W. 1988. Removal of phytic acid from soybean and cotton seed meals by A. ficuum phytase. J. Agric. Food Chem. 36: 1181–1183.
   Web of Science ®Google Scholar
• Han, Y. W. and Gallagher, D. J. 1987. Phytase production by Aspergillus ficuum on semi-solid substrate. J. Ind. Microbiol. 2: 195–200.
   Google Scholar
• Han, Y., Wilson, D. B., and Lei, X. G. 1999. Expression of an Aspergillus niger phytase gene (phy A) in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 65 (5): 1915–1918.
   Google Scholar
• Harland, B. F. and Morris, E. R. 1995. Phytate: A good or a bad food component. Nutr. Res. 15(5): 733–754.
   Web of Science ®Google Scholar
• Hemrika, W., Renirie, R., Dekker, H. L., Barnett, P., and Weaver, R. 1997. From phosphatases to vanadium peroxidases: A similar architechture of the active site. Proc. Natl. Acad. Sci. USA 94: 2145–2149.
   Google Scholar
• Howson, S. J. and Davis, R. P. 1983. Production of phytate hydrolysing enzymes by some fungi. Enz. Microb. Technol. 5: 377–389.
   Web of Science ®Google Scholar
• Ichibiki. 1995. Phytase and its preparation. Japan Pat. 07 059 562.
   Google Scholar
• Igbal, T. H., Lewis, K. O., and Cooper B. T. 1994. Phytase activity in the human and rat small intestine. Gut 35: 1233–236.
   Google Scholar
• Irving, G. C. J. and Cosgrove, D. J. 1971. Inositol phosphate phosphatases of microbiological origin. Some properties of a partially purified bacterial (Pseudomonas sp.) phytase. Aust. J. Biol. Sci. 24: 547–557.
   PubMedGoogle Scholar
• Irving, G. C. J. and Cosgrove, D. J. 1974. Inositol phosphate phosphatases of microbiological origin. Some properties of the partially purified phosphatases of Aspergillus ficuum NRRL 3135. Aust. J. Biol. Sci. 27: 361–368.
   PubMedGoogle Scholar
• Jareonkitmongkol, S., Ohya, M., Watanbe, R., Takagi, H., and Nakamori, S. 1997. Partial purification of phytase from a soil isolate bacterium, Klebsiella oxytoca MO-3. J. Ferm. Bioeng. 83 (4): 393–394.
   Google Scholar
• Johnson, L. F. and Tate, M. E. 1969. The structure of myo-inositol pentaphosphates. Ann. N. Y. Acad. Sci. 165: 526–532.
   PubMed Web of Science ®Google Scholar
• Kerovuo, J., Lappalainen, I., and Reinikainen, T. 2000. The metal dependence of Bacillus subtilis phytase. Biochim. Biophys. Res. Commun. 268 (2): 365–9.
   PubMed Web of Science ®Google Scholar
• Kerovuo, J., Lauraeus, M., Nurminen, P., Kalkkinen, N., and Apajalahti, J. 1998. Isolation, characterization, molecular gene cloning and sequencing of a novel phytase from Bacillus subtilis. Appl. Environ. Microbiol. 64: 2079–2085.
   PubMed Web of Science ®Google Scholar
• Khare, S. K., Jha, K., and Gupta, M. N. 1994. Entrapment of wheat phytase in polyacrylamide gel and its application in soy milk phytate hydrolysis. Biotechnol. Appl. Biochem. 19: 193–198.
   Web of Science ®Google Scholar
• Kim, Y. O., Kim, H. K., Bae, K. S., Yu, J. H., and Oh, T. K. 1998. Purification and properties of a thermostable phytase from Bacillus sp. DS11. Enz. Microb. Technol. 22: 2–7.
   Web of Science ®Google Scholar
• Knorr, D., Watkins, T. R., and Carlson, B. L. 1981 Enzymatic reduction of phytate in whole wheat breads. J. Food Sci. 46: 1866–1869.
   Web of Science ®Google Scholar
• Kostrewa, D., Gruninger-Leitch, F., D’Arcy, A., Broger, C., Mitchell, D., and van Loon, A. P. G. M. 1997. Crystal structure of phytase from Aspergillus ficuum at 2.5 Å resolution. Nat. Struct. Biol. 4: 185–190.
   Google Scholar
• Laboure, A. M., Gagnon, J., and Lescure, A. M. 1993. Purification and characterization of a phytase (myoinositol hexakisphosphate phosphohydrolase) accumulated in maize (zea mays) seedlings during germination. Biochem. J. 295: 413–419.
   PubMed Web of Science ®Google Scholar
• Lambrechts, C., Boze, H., Moulin, G., and Galzy, P. 1992. Utilization of phytate by some yeasts. Biotechnol. Lett. 14(1): 63–66.
   Google Scholar
• Lamosa, P., Burke, A., Peist, R., Huber, R., Liu, M. Y., Silva, G. , Rodrigues-Pousada, C., Legall, J., Maycock, C., and Santos, H. 2000. Thermostabilization of proteins by diglycerol phosphate, a new compatible solute from the hyperthermophile Archaeoglobus fulgidus. Appl. Environ. Microbiol. 66: 1974–1979.
   PubMed Web of Science ®Google Scholar
• Lassen, S. F., Bech, L., Fuglsang, C. C., Breinholt, J., Ohmann, A., and Ostergaard, P. R. 1997. “Phytase polypeptides.” International patent application, No. W098/28408.
   Google Scholar
• Laumen, K. and Ghisalba, O. 1994. Preparative scale chemo enzymatic synthesis of optically pure d-myo-inositol 1–phosphate. Biosci. Biotech. Biochem. 58: 2046–2049.
   PubMed Web of Science ®Google Scholar
• Li, J., Hegeman, C. E., Hanlon, R. W., Lacy, G. H., Denbow, D. M., and Grabau, E. A. 1997. Secretion of active recombinant phytase from soybean cell-suspension cultures. Plant Physiol. 114: 19.
   Google Scholar
• Liu, B., Rafiq, A., Tzeng, Y., and Rob, A. 1998. The induction and characterization of phytase and beyond. Enz. Microb. Technol. 22: 415–424.
   Web of Science ®Google Scholar
• Maga, J. A. 1982. Phytate: its chemistry, occurrence, food interactions, nutritional significance, and methods of analysis. J. Agric. Food Chem. 30: 1–9.
   Web of Science ®Google Scholar
• Maugenest, S., Martinez, I., and Lescure, A. M. 1997. Cloning and characterization of a cDNA encoding a maize seedling phytase. Biochem. J. 322: 511–517.
   Google Scholar
• Mayer, A. F., Hellmuth, K., Schlieker, H., Lopez – Ulibarri, R., Oertel, S., Dahlems, U., Strasser, A. W., and van Loon, A. P. 1999. An expression system matures: a highly efficient and cost effective process for phytase production by recombinant strains of Hansenula polymorpha. Biotechnol. Bioeng. 63(3): 373–381.
   Google Scholar
• Mc collum, E. V. and Hart, E. B. 1908. On the occurrence of a phytin splitting enzyme in animal tissue. J. Biol. Chem. 4: 497–500.
   Google Scholar
• Mellanby, E. 1949. The rickets producing and anticalcifying action of phytate. J. Physiol. (London) 109: 488–493.
   Google Scholar
• Mitchell, D. B., Vogel, K., Weimann, B. J., Pasamontes, L., and van Loon, A. P. 1997. The phytase subfamily of histidine acid phosphatase; isolation of genes for two novel phytases from the Aspergillus terreus and Myceliophthora thermophila. Microbiology. 143: 245–252.
   PubMed Web of Science ®Google Scholar
• Mohanna, C. and Nys, Y. 1999. Changes in zinc and manganese availability in broiler chicks induced by vegetal and microbial phytases. Anim. Feed Sci. Technol. 77: 241–253.
   Web of Science ®Google Scholar
• Moore, E., Helly, V. R., Conneely, O. M., Ward, P. P., Power, R. F., and Headon, D. R. 1995. Molecular cloning, expression and evaluation of phosphohydrolases for phytate degrading activity. J. Ind. Microbiol. 14: 396–402.
   Google Scholar
• Mullaney, E. J., Daly, C. B., and Ullah, A. H. J. 2000. Advances in phytase research. Adv. Appl. Microbiol. 47: 157–199.
   PubMed Web of Science ®Google Scholar
• Mullaney, E. J., Gibson, D. M., and Ullah, A. H. J. 1991. Positive identification of a X gt11 clone containing a region of fungal phytase gene by immunoprobe and sequence verification. Appl. Microbiol. Biotechnol. 35: 611–614.
   PubMed Web of Science ®Google Scholar
• Mwachireya, S. A., Beames, R. M., Higgs, D. A., and Dosanjh, B. S. 1999. Digestibility of canola protein products derived from the physical, enzymatic and chemical processing of commercial canola meal in rainbow trout Oncorhynchus mykiss (Walbaum) held in fresh water. Aquacul. Nutr. 5: 73–82.
   Web of Science ®Google Scholar
• Nakamura, Y., Fukuhara, H., and Sano, K. 2000. Secreted phytase activities of yeasts. Biosci. Biotechnol. Biochem. 64 (4): 841–844.
   PubMed Web of Science ®Google Scholar
• Nair, V. C. and Duvnjak, Z. 1990. Reduction of phytic acid content in canola meal by Aspergillus ficuum in solid state fermentation process. Appl. Microbiol. Biotechnol. 34: 183–188.
   Web of Science ®Google Scholar
• Nair, V. C., Laflamme, J., and Duvnjak, Z. 1991. Production of phytase by Aspergillus ficuum and reduction of phytic acid content in canola meal. J. Sci. Food Agric. 54: 356–365.
   Google Scholar
• Nayini, N. R. and Markakis, P. 1984. The phytase of yeast. Lebensm. Wiss. Technol. 17: 24–26.
   Google Scholar
• Nelson, T. S. 1967. The utilization of phytate phosphorus by poultry. Poult. Sci. 46: 862–871.
   PubMed Web of Science ®Google Scholar
• Nelson, T. S., Sheih, T. R., Wodzinski, R. J., and Ware, J. H. 1971. Effect of supplement phytase on the utilizaion of phytate phosphorus by chicks. J. Nutr. 101: 1289–1294.
   PubMed Web of Science ®Google Scholar
• Nelson, T. S., Shieh, T. R., Wodzinski, R. J., and Ware, J. H. 1968. The availability of phytate phosphorus in soybean meal before and after treatment with a mold phytase. Poult. Sci. 47: 1842–1848.
   PubMed Web of Science ®Google Scholar
• Ngashima, T., Tange, T., and Anazawa, H. 1999. Dephosphorylation of phytate by using Aspergillus niger phytase with a high affinity for phytate. Appl. Environ. Microbiol. 65(10): 4682–4684.
   Google Scholar
• Novo Nordisk A/S. 1999. New phytase could make a world of difference. BioTimes 14(3): 6–7.
   Google Scholar
• O’Dell, B. L. and Savage, J. E. 1960. Effect of phytic acid on zinc availability. Proc. Soc. Exp. Biol. Med. 103: 304.
   PubMed Web of Science ®Google Scholar
• O’Quinn, P. R., Knabe, D. A., and Gregg, E. J. 1997. Efficacy of Natuphos in sorghum-based diets of finishing swine. J. Anim. Sci. 75: 1299–1307.
   PubMed Web of Science ®Google Scholar
• Ostanin, K., Harms, E., Stevis, P. E., Kuciel, R., Zhou, M. M., and van Etten, R. L. 1992. Overexpression, site directed mutagenesis, and mechanism of Escherichia coli acid phosphatase. J. Biol. Chem. 267: 22830–22836.
   PubMed Web of Science ®Google Scholar
• Panda, A. K., Reddy, M. R., Rao, S. V. R., and Praharaj, N. K. 1998. The role of yeast culture Saccharomyces cerevisiae as feed additive in poultry. Poult. Punch. 25–27.
   Google Scholar
• Pasamontes, L., Haiker, M., Wyss, M., Tessier, M., and van Loon, A. P. G. M. 1997. Gene cloning, purification and characterization of a heat stable phytase from the fungus Aspergillus fumigatus. Appl. Environ. Microbiol. 63(5): 1696–1700.
   PubMed Web of Science ®Google Scholar
• Patwardhan, V. N. 1937. The occurrence of a phytin splitting enzyme in the intestines of albino rats. Biochem. J. 31: 560–564.
   Google Scholar
• Pen, J., Verwoerd, T. C., van Paridon, P.A., Beudeker, R. F., and van den Elzen, P. J. M. 1993. Phytase containing transgenic seeds as a novel feed additive for improved phosphorus utilization. Bio/Technol. 11: 811–814.
   Web of Science ®Google Scholar
• Pen, J., Verwoerd, T. C., van Paridon, P.A., van Coyen, A. J. J., van den Elzen, P. J. M., and Hoekema, A. 1994. Production of high value proteins in plants. J. Cell. Biochem. 18A: 77.
   Google Scholar
• Pfeffer, E. 1993. cited in D. C. Billington: The Inositol Phosphates. Chemical Synthesis and Biological Significance. Verlag Chemie, Weinheim.
   Google Scholar
• Piddington, C. S., Houston, C. S., Palobeimo, M., Cantrell, M., Micttinen-Oinonen, A., Nevalinen, H., and Ram Bosek, J. 1993. The cloning and sequencing of the genes encoding phytase (phyA) and pH 2.5 optimum acid phosphatase (aph) from Aspergillus niger var. awamorii. Gene 133: 5562.
   Google Scholar
• Posternak 1903. Compt. Rend. 137, 202. Phytase. In: Advances in Applied Microbiology, 1996. 42: 263–302.
   Google Scholar
• Powar, V. K. and Jagannathan, V. 1967. Phytase from Bacillus subtilis. Indian J. Biochem. 4: 184–185.
   PubMedGoogle Scholar
• Powar, V. K. and Jagannathan, V. 1982. Purification and properties of phytate specific phosphatase from Bacillus subtilis. J. Bacteriol. 151: 1102–1108.
   PubMed Web of Science ®Google Scholar
• Quan, C. S., Zhang, L. H., Wang, Y. J., and Ohta, Y. Y. 2001. Production of phytase in a low phosphate medium by a novel yeast Candida krusei. J. Biosci. Bioeng. 92(2): 154–160.
   Google Scholar
• Raboy, V. and Gerbasi, P. 1996. Genetics of myoinositol phosphate synthesis and accumulation. In “Subcellular Biochemistry.” Vol. 26: myoinositol phosphates, phosphoinositides, and signal transduction, pp. 257–285. Biswas, B. B., and Biswas, S., Eds., Plenum Press, New York.
   Google Scholar
• Rapoport, S., Leva, E., and Guest, G. M. 1941. Phytase in plasma and erythrocytes of vertebrates. J. Biol. Chem. 139: 621–632.
   Google Scholar
• Robinson, E. H., Jackson, S., and Li, M. H. 1996. Supplemental phytase in catfish diets. Aquacul. Mag. 22: 80–82.
   Google Scholar
• Rodriguez, E., Mullaney, E. J., and Lei, X. G. 2000. Expression of Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of recombinant enzyme. Biochem. Biophys. Res. Commun. 268 (2): 373–8.
   Google Scholar
• Rodriguez, E., Porres, J. M., Han, Y., and Lei, X. G. 1999. Different sensitivity of recombinant Aspergillus niger (r-Phy A) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro. Arch. Biochem. Biophys. 365(2): 262–267.
   Google Scholar
• Rumsey, G. L. 1993. Fish meal and alternate sources of protein in fish feeds: Update, Fisheries 18: 14–19.
   Web of Science ®Google Scholar
• Sandberg, A. S., Hulthen, L. R., and Turk, M. 1996. Dietary Aspergillus niger phytase increases iron absorption in humans. J. Nutr. 126: 476–480.
   PubMed Web of Science ®Google Scholar
• Sandberg, A. S., Larsen, T., and Sandstorm, B. 1993. High dietary calcium level decreases phytate degradation in pigs fed a rapeseed diet. J. Nutr. 123: 559–566.
   PubMed Web of Science ®Google Scholar
• Sano, K., Fukuhara, H., and Nakamura, Y. 1999. Phytase of the yeast Arxula adeninivorans. Biotechnol. Lett. 21: 33–38.
   Web of Science ®Google Scholar
• Scott, N. and Steven, D. 2000. Engineering a disulfide bond in recombinant manganese peroxidase results in increased thermostability. Biotechnol. Prog. 16: 326–333.
   Google Scholar
• Sebastian, S., Touchburn, S. P., Chavez, E. R., and Lague, P. C. 1996. The effect of supplemental phytase on the performance and utilization of dietary calcium, phosphorus, copper and zinc in broiler chickens fed corn soybean diets. Poult. Sci. 76: 729–736.
   Google Scholar
• Segueilha, L., Lambrechts, C., Boze, H., Moulin, G., and Galzy, P. 1992. Purification and properties of the phytase from Schwanniomyces castellii. J. Ferment. Bioeng. 74(1): 7–11.
   Google Scholar
• Segueilha, L., Moulin, G., and Galzy, P. 1993. Reduction of phytate content in wheat bran and glandless cotton flour by Schwanniomyces castellii. J. Agric. Food Chem. 41: 2451–2454
   Google Scholar
• Shieh, T.R. and Ware, J. H. 1968. Survey of microorganisms for the production of extracellular phytase. Appl. Microbiol. 169(9): 1348–1351.
   Google Scholar
• Shieh, T. R., Wodzinski, R. J., and Ware, J. H. 1969. Regulation of the formation of acid phosphatase by inorganic phosphate in Aspergillus ficuum. J. Bacteriol. 100: 1161–1165.
   PubMed Web of Science ®Google Scholar
• Shimizu, M. 1992. Purification and characterization of phytase from Bacillus subtilis (natto) N-77. Biosci. Biotechnol. Biochem. 56(8): 1266–1269.
   PubMed Web of Science ®Google Scholar
• Simell, M., Turunen, M., Piironen, J., and Vaara, T. 1989. Feed and food applications of phytase. Lecture at 3rd Meet. Industrial Applications of Enzymes, Barcelona (Spain).
   Google Scholar
• Simons, P. C. M., Versteegh, H. A. J., Jongbloed, A. W., Kemme, P. A., Slump, P., Bos, K. D., Wolters, M. G. E., Beudeker, R. F., and Verschoor, G. J. 1990. Improvement of phosphorus availability by microbial phytase in broilers and pigs. Br. J. Nutr. 64: 525–540.
   PubMed Web of Science ®Google Scholar
• Siren, M. 1986a. Stabilized pharmaceutical and biological material composition. Pat. SE 003 165.
   Google Scholar
• Siren, M. 1986b. New myo-inositol triphosphoric acid isomer. Pat. SW 052 950.
   Google Scholar
• Skowronaski, T. 1978. Some properties of partially purified phytase from Aspergillus niger. Acta Micro. Pol. 27: 41–48.
   Google Scholar
• Spitzer, R. S. and Phillips, P. H. 1972. Cited in K. Bitar, J. G. Reinhold. Phytase and alkaline phosphatase activities in intestinal mucosae of rat, chicken, calf and man. Biochim. Biophys. Acta 268: 442–452.
   Google Scholar
• Sreeramulu, G., Srinivasa, D. S., Nand, K., and Joseph, R. 1996. Lactobacillus amylovorus as a phytase producer in submerged culture. Lett. Appl. Microbiol. 23: 385–388.
   Web of Science ®Google Scholar
• Stahl, C. H., Roneker, K. R., Thornton, J. R., and Lei, X. G. 2000. A new phytase in yeast effectively improves the bioavailability of phytate phosphorus to weanling pigs. J. Anim. Sci. 78 (3): 668–674.
   Google Scholar
• Sutardi, M. and Buckle, K. A. 1988. Characterization of extra and intracellular phytase from Rhizopus oligosporus used in tempeh production. Int. J. Food Microbiol. 6: 67–69.
   PubMed Web of Science ®Google Scholar
• Suzuki, U., Yoshimura, K., and Takaishi, M. 1907. Ueber ein Enzym “Phytase” das “Anhydro-oxymethylen diphosphorsaure” Spaltet. Tokyo Imper. Univ. Coll. Agric. Bull. 7: 503–512.
   Google Scholar
• Tambe, S. M., Kakli, S. G., Kelkar, S. M., and Parekh, L. J. 1994. Two distinct molecular forms of phytase from Klebsiella aerogenes: Evidence for unusually small active enzyme peptide. J. Ferm. Bioeng. 77(1): 23–27.
   Google Scholar
• Tomschy, A., Wyss, M., Kostrewa, D., Vogel, K., Tessier, M., Hofer, S., Burgin, H., Kronenberg, A., Remy, R., and van Loon, A.P.G.M. 2000a. Active site residue 297 of Aspergillus niger phytase critically affects the catalytic properties. FEBS Lett. 472: 169–172.
   Google Scholar
• Tomschy, A., Tessier, M., Wyss, M., Brugger, R., Broger, R., Shnoebelen, L., van Loon, A. P. G. M., and Pasamontes, L. 2000b. Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three dimensional structure. Protein Sci. 9: 1304–1311.
   PubMed Web of Science ®Google Scholar
• Tomschy, A., Brugger, R., Lehmann, M., Svendsen, A., Vogel, K., Kostrewa, D., Lassen, S. F., Burger, D., Kronenberger, A., van Loon, A. P. G. M., Pasamontes, L., and Wyss, M. 2002. Engineering of phytase for improved activity at low pH. Appl. Environ. Microbiol. 68: 1907–1913.
   PubMed Web of Science ®Google Scholar
• Thompson, L. U. and Yoon, J. H. 1984. Starch digestibility as affected by polyphenols and phytic acid. J. Food Sci. 49: 1228–1229.
   Web of Science ®Google Scholar
• Tyagi, P. K., Tyagi, P. K., and Verma, S. V. S. 1998. Phytate phosphorus content of some common poultry feed stuffs. Indian J. Poult. Sci. 33(1): 86–88.
   Google Scholar
• Ullah, A. H. J. and Cummins, B. J. 1988. A. ficuum extracellular phytase: Immobilization on glutaraldehyde-activated silicate. Ann. N. Y. Acad. Sci. 542: 102–106.
   Google Scholar
• Ullah, A. H. J., Cummins, B. J., and Dischinger, H. C., Jr. 1991. Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytase. Biochem. Biophys. Res. Commun. 178: 45–53.
   Google Scholar
• Ullah, A. H. J. and Dischinger, H. C., Jr. 1992. Identification of residues involved in active site formation in A. ficuum phytase. Ann. N. Y. Acad. Sci. 672: 45–51.
   Google Scholar
• Ullah, A. H. J. and Dischinger, H. C. 1993. Aspergillus ficuum phytase: complete primary structure elucidation by chemical sequencing. Biochem. Biophys. Res. Commun. 192: 747–753.
   PubMed Web of Science ®Google Scholar
• Ullah, A. H. J. and Gibson, D. M. 1987. Extracellular phytase (EC 3.1.3.8) from Aspergillus ficuum NRRL 3135: purification and characterization. Prep. Biochem. 17: 63–91.
   PubMed Web of Science ®Google Scholar
• Ullah, A. H. J. and Mullaney, E. J. 1996. Disulfide bonds are necessary for structure and activity in Aspergillus ficuum phytase. Biochem. Biophys. Res. Commun. 227 (2): 311–317.
   Google Scholar
• Ullah, A. H. and Phillippy, B. Q. 1988. Immobilization of Aspergillus ficuum phytase: product characterization of the bioreactor. Prep. Biochem. 18 (4): 483–9.
   Web of Science ®Google Scholar
• Ullah, A. H., Sethumadhavan, K., Mullaney, E. J., Ziegelhoffer, T., and Austin-Phillips, S. 1999. Characterization of recombinant fungal phytase (phy A) expressed in tobacco leaves. Biochem. Biophys. Res. Commun. 264 (1): 201–206.
   Google Scholar
• Ullah, A. H., Sethumadhavan, K., Mullaney, E. J., Ziegelhoffer, T., and Austin-Phillips, S. 2002. Cloned and expressed fungal phyA gene in alfalfa produces a stable phytase. Biochem. Biophys. Res. Commun. 290: 1343–1348.
   PubMed Web of Science ®Google Scholar
• Van de Velde, F., Konemann, L., van Rantwijk, F., and Sheldon, R. A. 2000. The rational design of semisynthetic peroxidases. Biotechnol. Bioeng. 67: 87–96.
   Google Scholar
• Van Dijck, P. W. M. 1999. Chymosin and phytase, made by genetic engineering. J. Biotechnol. 67: 77–80.
   Google Scholar
• Van Etten, R. L. 1982. Human prostatic acid phosphatase: a histidine phosphatase. Ann. N.Y. Acad. Sci. 390: 27–51.
   Google Scholar
• Van Etten, R. L., Davidson, R., Stevis, P. E., MacArthur, H., and Moore, D. L. 1991. Covalent structure, disulfide bonding and identification of reactive surface and active site residues of human prostatic acid phosphatase. J. Biol. Chem. 266: 2313–2319.
   Google Scholar
• Van Hartinsveldt, W., van Zeijl, C. M., Harteeld, G. M., Gouka, R. J., Suykerbuyk, M. E., Luiten, R. G., van Paridon, P. A., Selten, G. C., Veenstra, A. E., van Gorcom, R. F. M., and van den Hondel, C. A. M. J. J. 1993. Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger. Gene 127: 87–94.
   Google Scholar
• Vohra, A. and Satyanarayana, T. 2001. Phytase production by the yeast Pichia anomala. Biotechnol. Lett. 23(7): 551–554.
   Google Scholar
• Vohra, A. and Satyanarayana, T. 2002a. Statistial optimization of the medium components by response surface methodology to enhance phytase production by Pichia anomala. Process Biochem. 37: 999–1004.
   Web of Science ®Google Scholar
• Vohra, A. and Satyanarayana, T. 2002b. Purification and characterization of a thermostable and acidstable phytase from Pichia anomala. World J. Microbiol. Biotechnol. 18: 687–691.
   Web of Science ®Google Scholar
• Walsh, G. A., Power, R. F., and Headon, D. R. 1993. Enzymes in the animal feed industry. TIBTECH 11: 424–430.
   PubMed Web of Science ®Google Scholar
• Wang, H. L., Savain, W., and Hesseltine, C.W. 1980. Phytase of molds used in oriental food fermentation. J. Food Sci. 45: 1261–1266.
   Google Scholar
• Watanbe, K. and Suzuki, Y. 1998. Protein thermostabilization by proline substitutions. J. Mol. Cat. B: Enzymatic 4: 167–180.
   Google Scholar
• Whitelam, G. C. 1995. The production of recombinant proteins in plants. J. Sci. Food Agric. 68: 1–9.
   Google Scholar
• Wodzinski, R. J. and Ullah, A. H. J. 1996. Phytase. Adv. Appl. Microbiol. 42: 263–302.
   PubMed Web of Science ®Google Scholar
• Wyss, M. R., Brugger, R., Kronenberger, A., Remy, R., Fimbel, R., Oesterhelt, G., Lehmann, M. and van Loon, A. P. G. M. 1999. Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties. Appl. Environ. Microbiol. 65: 367–373.
   PubMed Web of Science ®Google Scholar
• Wyss, M., Pasamontes, L., Remy, R., Kohler, J., Kusznir, E., Gadient, M., Muller, F., and Van loon, A. P. G. M. 1998. Comparison of thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase and A. niger pH 2.5 acid phosphatase. Appl. Environ. Microbiol. 64: 4446–4451.
   PubMed Web of Science ®Google Scholar
• Yamada, K., Minoda, Y., Kobayashi, T., Hidaka, Y., Matuo, H., and Kobayashi, M. 1968. Phytase from Aspergillus terreus I production, purification and some general properties of the enzyme. Agric. Biol. Chem. 32: 1275–1282.
   Web of Science ®Google Scholar
• Yanke, L. J., Bae, H. D., Selinger, L. B., and Cheng, K. J. 1998. Phytase activity of anaerobic ruminal bcteria. Microbiology 144: 1565–1573.
   PubMed Web of Science ®Google Scholar
• Yanke, L. J., Selinger, L. B., and Cheng, K. J. 1999. Phytase activity of Selenomonas ruminantium: a preliminary characterization. Lett. Appl. Microbiol. 29: 20–25.
   Web of Science ®Google Scholar
• Yi, Z., Kornegay, E. T., and Denbow, D. M. 1997. Supplemental microbial phytase improves zinc utilization in broilers. Poult. Sci. 75: 540–546.
   Google Scholar
• Yi, Z., Kornegay, E. T., Ravindran, V., and Denbow D. M. 1996. Improving phytate phosphorus availability in corn and soybean meal for broilers using microbial phytase and calculation of phosphorus equivalency values for phytase. Poult. Sci. 75: 240–249.
   PubMed Web of Science ®Google Scholar
• Yoon, S. J., Choi, Y. J., Min, H. K., Cho, K. K., Kim, J. W., Zee, S. C., and Jung, Y. H. 1996. Isolation and identification ofphytase producing bacterium, Enterobacter sp. 4 and enzymatic properties of phytase enzyme. Enz. Microb. Technol. 18: 449–454.
   Web of Science ®Google Scholar
• Zyta, K. and Gogol, D. 2002. In vitro efficacies of phosphorolytic enzymes synthesized in mycelial cells of Aspergillus niger AbZ4 grown by a liquid surface fermentation. J. Agric. Food Chem. 50(4): 899–905.
   Google Scholar
• Zyta, K., Koreleski, J., and Kujawski, M. 1989. Dephosphorylation of phytate compounds by means of acid phosphatase from Aspergillus niger. J. Sci. Food Agric. 49:315–324.
   Google Scholar