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Volumn 2, Issue , 2010, Pages 96-128

Phytases: Biochemistry, enzymology and characteristics relevant to animal feed use

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EID: 84861863739     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (57)

References (174)
  • 1
    • 0029401110 scopus 로고
    • Phytase-induced changes in mineral utilization in zinc-supplemented diets for pigs
    • Adeola, O., Lawrence, B.V., Sutton A.L. and Cline, T.R. (1995) Phytase-induced changes in mineral utilization in zinc-supplemented diets for pigs. Journal of Animal Science 73, 3384-3391.
    • (1995) Journal of Animal Science , vol.73 , pp. 3384-3391
    • Adeola, O.1    Lawrence, B.V.2    Sutton, A.L.3    Cline, T.R.4
  • 2
    • 34248581722 scopus 로고    scopus 로고
    • Response of growing pigs to Peniophora lycii-and Escherichia coli-derived phytases or varying ratios of calcium to total phosphorus
    • Adeola, O., Olukosi, O.A., Jendza, J.A., Dilger, R.N. and Bedford, M.R. (2006) Response of growing pigs to Peniophora lycii-and Escherichia coli-derived phytases or varying ratios of calcium to total phosphorus. Animal Science 82, 637-644.
    • (2006) Animal Science , vol.82 , pp. 637-644
    • Adeola, O.1    Olukosi, O.A.2    Jendza, J.A.3    Dilger, R.N.4    Bedford, M.R.5
  • 3
    • 8344239556 scopus 로고    scopus 로고
    • Metabolism of extracellular inositol hexaphosphate (phytate) by Saccharomyces cerevisiae
    • Andlid, T.A., Veide, J. and Sandberg, A.-S. (2004) Metabolism of extracellular inositol hexaphosphate (phytate) by Saccharomyces cerevisiae. International Journal of Food Microbiology 97, 157-169.
    • (2004) International Journal of Food Microbiology , vol.97 , pp. 157-169
    • Andlid, T.A.1    Veide, J.2    Sandberg, A.-S.3
  • 4
    • 1542393027 scopus 로고    scopus 로고
    • Efficacy of a phytase derived from Escherichia coli and expressed in yeast on phosphorus utilization and bone mineralization in turkey poults
    • Applegate, T.J., Webel, D.M. and Lei, X.G. (2003) Efficacy of a phytase derived from Escherichia coli and expressed in yeast on phosphorus utilization and bone mineralization in turkey poults. Poultry Science 82, 1726-1732.
    • (2003) Poultry Science , vol.82 , pp. 1726-1732
    • Applegate, T.J.1    Webel, D.M.2    Lei, X.G.3
  • 5
    • 0028106110 scopus 로고
    • Role of the transcriptional activator AppY in regulation of the cyx-appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase
    • Atlung, T. and Brøndsted, L. (1994) Role of the transcriptional activator AppY in regulation of the cyx-appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase. Journal of Bacteriology 176, 5414-5422.
    • (1994) Journal of Bacteriology , vol.176 , pp. 5414-5422
    • Atlung, T.1    Brøndsted, L.2
  • 6
    • 0030609822 scopus 로고    scopus 로고
    • Effects of sS and the transcriptional activator AppY on induction of Escherichia coli hya and cbdAB-appA operons in response to carbon and phosphate starvation
    • Atlung, T., Knudsen, K., Heerfordt, L. and Brøndsted, L. (1997) Effects of sS and the transcriptional activator AppY on induction of Escherichia coli hya and cbdAB-appA operons in response to carbon and phosphate starvation. Journal of Bacteriology 179, 2141-2146.
    • (1997) Journal of Bacteriology , vol.179 , pp. 2141-2146
    • Atlung, T.1    Knudsen, K.2    Heerfordt, L.3    Brøndsted, L.4
  • 7
    • 0037528980 scopus 로고    scopus 로고
    • Efficacy of an E. coli phytase expressed in yeast for releasing phytate-bound phosphorus in young chicks and pigs.
    • Augspurger, N.R., Webel, D.M., Lei, X.G. and Baker, D.H. (2003) Efficacy of an E. coli phytase expressed in yeast for releasing phytate-bound phosphorus in young chicks and pigs. Journal of Animal Science 81, 474-483.
    • (2003) Journal of Animal Science , vol.81 , pp. 474-483
    • Augspurger, N.R.1    Webel, D.M.2    Lei, X.G.3    Baker, D.H.4
  • 8
    • 0001251469 scopus 로고
    • Localization of constitutive phytases in lily pollen and properties of the pH 8 form
    • Baldi, B.G., Scott, J.J., Everard, J.D. and Loewus, F.A. (1988) Localization of constitutive phytases in lily pollen and properties of the pH 8 form. Plant Science 56, 137-147.
    • (1988) Plant Science , vol.56 , pp. 137-147
    • Baldi, B.G.1    Scott, J.J.2    Everard, J.D.3    Loewus, F.A.4
  • 9
    • 0028675620 scopus 로고
    • Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen
    • Barrientos, L., Scott, J.J. and Murthy, P.P. (1994) Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen. Plant Physiology 106, 1489-1495.
    • (1994) Plant Physiology , vol.106 , pp. 1489-1495
    • Barrientos, L.1    Scott, J.J.2    Murthy, P.P.3
  • 10
    • 0031793334 scopus 로고    scopus 로고
    • Molecular characterization and expression of a phytase gene from the thermophilic fungus Thermomyces lanuginosus
    • 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. Applied and Environmental Microbiology 64, 4423-4427.
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 4423-4427
    • Berka, R.M.1    Rey, M.W.2    Brown, K.M.3    Byun, T.4    Klotz, A.V.5
  • 11
    • 0142245644 scopus 로고    scopus 로고
    • PhyA, a secreted protein of Xanthomonas oryzae pv. oryzae, is required for optimum virulence and growth on phytic acid as a sole phosphate source.
    • Chatterjee, S., Sankaranarayanan, R. and Sonti, R.V. (2003) PhyA, a secreted protein of Xanthomonas oryzae pv. oryzae, is required for optimum virulence and growth on phytic acid as a sole phosphate source. Molecular Plant-Microbe Interaction 16, 973-982.
    • (2003) Molecular Plant-Microbe Interaction , vol.16 , pp. 973-982
    • Chatterjee, S.1    Sankaranarayanan, R.2    Sonti, R.V.3
  • 12
    • 33644535130 scopus 로고    scopus 로고
    • Beta-propeller phytases in the aquatic environment
    • Cheng, C. and Lim, B.L. (2006) Beta-propeller phytases in the aquatic environment. Archives of Microbiology 185, 1-13.
    • (2006) Archives of Microbiology , vol.185 , pp. 1-13
    • Cheng, C.1    Lim, B.L.2
  • 14
    • 0041861334 scopus 로고    scopus 로고
    • Purification and characterization of a phytase from Pseudomonas syringae MOK1
    • Cho, J.S., Lee, C.W., Kang, S.H., Lee, J.C., Bok, J.D., Moon, Y.S. et al. (2003) Purification and characterization of a phytase from Pseudomonas syringae MOK1. Current Microbiology 47, 290-294.
    • (2003) Current Microbiology , vol.47 , pp. 290-294
    • Cho, J.S.1    Lee, C.W.2    Kang, S.H.3    Lee, J.C.4    Bok, J.D.5    Moon, Y.S.6
  • 15
    • 0034815761 scopus 로고    scopus 로고
    • Purification and properties of extracellular phytase from Bacillus sp. KHU-10.
    • Choi, Y.M., Suh, H.J. and Kim, J.M. (2001) Purification and properties of extracellular phytase from Bacillus sp. KHU-10. Journal of Protein Chemistry 20, 287-292.
    • (2001) Journal of Protein Chemistry , vol.20 , pp. 287-292
    • Choi, Y.M.1    Suh, H.J.2    Kim, J.M.3
  • 16
    • 7944229708 scopus 로고    scopus 로고
    • Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis
    • Chu, H.M., Guo, R.T., Lin, T.W., Chou, C.W., Shr, H.L., Lai, H.L. et al. (2004) Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis. Structure 12, 2015-2024.
    • (2004) Structure , vol.12 , pp. 2015-2024
    • Chu, H.M.1    Guo, R.T.2    Lin, T.W.3    Chou, C.W.4    Shr, H.L.5    Lai, H.L.6
  • 17
    • 0014915828 scopus 로고
    • Inositol phosphate phosphatase of microbiological origin. Inositol pentaphosphate intermediates in the dephosphorylation of the hexaphosphates of myoinositol. scyllo-inositol, and D-chiro-inositol, by a bacterial (Pseudomonas sp.) phytase
    • Cosgrove, D.J. (1970) Inositol phosphate phosphatase of microbiological origin. Inositol pentaphosphate intermediates in the dephosphorylation of the hexaphosphates of myoinositol, scyllo-inositol, and D-chiro-inositol, by a bacterial (Pseudomonas sp.) phytase. Australian Journal of Biological Sciences 23, 1207-1220.
    • (1970) Australian Journal of Biological Sciences , vol.23 , pp. 1207-1220
    • Cosgrove, D.J.1
  • 18
  • 19
    • 33748369099 scopus 로고    scopus 로고
    • Supplementation of corn-soy-based diets with an Escherichia coli-derived phytase: effects on broiler chick performance and the digestibility of amino acids and metabolizability of minerals and energy
    • Cowieson, A.J., Acamovic, T. and Bedford, M.R. (2006) Supplementation of corn-soy-based diets with an Escherichia coli-derived phytase: effects on broiler chick performance and the digestibility of amino acids and metabolizability of minerals and energy. Poultry Science 85, 1389-1397.
    • (2006) Poultry Science , vol.85 , pp. 1389-1397
    • Cowieson, A.J.1    Acamovic, T.2    Bedford, M.R.3
  • 20
    • 0141870038 scopus 로고    scopus 로고
    • Phytase activity in sourdough lactic acid bacteria: purification and characterization of a phytase from Lactobacillus sanfranciscensis CB1
    • De Angelis, M., Gallo, G., Corbo, M.R., McSweeney, P.L.H., Faccia, M., Giovine, M. et al. (2003) Phytase activity in sourdough lactic acid bacteria: purification and characterization of a phytase from Lactobacillus sanfranciscensis CB1. Food Microbiology 87, 259-270.
    • (2003) Food Microbiology , vol.87 , pp. 259-270
    • De Angelis, M.1    Gallo, G.2    Corbo, M.R.3    McSweeney, P.L.H.4    Faccia, M.5    Giovine, M.6
  • 22
    • 15444372458 scopus 로고    scopus 로고
    • Mineral status of Pangasius pangasius (Hamilton) fingerlings in relation to supplemental phytase; absorption, whole-body and bone mineral content
    • Debnath, D., Sahu, N.P., Pal, A.K., Jain, K.K., Yengkokpam, S. and Mukherjee, S.C. (2005b) Mineral status of Pangasius pangasius (Hamilton) fingerlings in relation to supplemental phytase; absorption, whole-body and bone mineral content. Aquaculture Research 36, 326-335.
    • (2005) Aquaculture Research , vol.36 , pp. 326-335
    • Debnath, D.1    Sahu, N.P.2    Pal, A.K.3    Jain, K.K.4    Yengkokpam, S.5    Mukherjee, S.C.6
  • 23
    • 0033964846 scopus 로고    scopus 로고
    • Phosphatases and kinases delivered to the host cell by bacterial pathogens
    • DeVinney, R., Steele-Morimer, O. and Finlay, B.B. (2000) Phosphatases and kinases delivered to the host cell by bacterial pathogens. Trends in Microbiology 8, 29-33.
    • (2000) Trends in Microbiology , vol.8 , pp. 29-33
    • DeVinney, R.1    Steele-Morimer, O.2    Finlay, B.B.3
  • 24
    • 33847203303 scopus 로고    scopus 로고
    • Wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) multiple inositol polyphosphate phosphatases (MINPPs) are phytases expressed during grain filling and germination
    • Dionisio, G., Holm, P.B. and Brinch-Pedersen, H. (2007) Wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) multiple inositol polyphosphate phosphatases (MINPPs) are phytases expressed during grain filling and germination. Plant Biotechnology Journal 5, 325-338.
    • (2007) Plant Biotechnology Journal , vol.5 , pp. 325-338
    • Dionisio, G.1    Holm, P.B.2    Brinch-Pedersen, H.3
  • 25
    • 0001135259 scopus 로고
    • The quantitative effects of an industrial microbial phytase and wheat phytase on the apparent phosphorus absorbability of a mixed feed by piglets
    • Eeckhout, W. and de Paepe, M. (1991) The quantitative effects of an industrial microbial phytase and wheat phytase on the apparent phosphorus absorbability of a mixed feed by piglets. Medical Faculty Landbouwwetenschappen Rijksuniversiteit Gent 56, 1643-1647.
    • (1991) Medical Faculty Landbouwwetenschappen Rijksuniversiteit Gent , vol.56 , pp. 1643-1647
    • Eeckhout, W.1    De Paepe, M.2
  • 26
    • 33847229126 scopus 로고    scopus 로고
    • In vitro and in vivo characteristics of bacterial phytases and their efficacy in broiler chickens
    • Elkhalil, E.A.I., Männer, K., Borriss, R. and Simon, O. (2007) In vitro and in vivo characteristics of bacterial phytases and their efficacy in broiler chickens. British Poultry Science 48, 64-70.
    • (2007) British Poultry Science , vol.48 , pp. 64-70
    • Elkhalil, E.A.I.1    Männer, K.2    Borriss, R.3    Simon, O.4
  • 28
    • 20444484150 scopus 로고    scopus 로고
    • Phosphorus equivalence of a consensus phytase produced by Hansenula polymorpha in diets for young turkeys
    • Esteve-Garcia, E., Perez-Vendrell, A.M. and Broz, J. (2005) Phosphorus equivalence of a consensus phytase produced by Hansenula polymorpha in diets for young turkeys. Archives of Animal Nutrition 59, 53-59.
    • (2005) Archives of Animal Nutrition , vol.59 , pp. 53-59
    • Esteve-Garcia, E.1    Perez-Vendrell, A.M.2    Broz, J.3
  • 29
    • 67650806136 scopus 로고    scopus 로고
    • Improvement of Yersinia frederiksenii phytase performance by a single amino acid substitution
    • Fu, D., Huang, H., Meng, K., Wang, Y., Luo, H., Yang, P. et al. (2009) Improvement of Yersinia frederiksenii phytase performance by a single amino acid substitution. Biotechnology and Bioengineering 103, 857-864.
    • (2009) Biotechnology and Bioengineering , vol.103 , pp. 857-864
    • Fu, D.1    Huang, H.2    Meng, K.3    Wang, Y.4    Luo, H.5    Yang, P.6
  • 30
    • 0033672641 scopus 로고    scopus 로고
    • Isolation and characterization of phytase isozymes produced by Aspergillus oryzae
    • Fujita, J., Budda, N., Tujimoto, M., Yamane, Y., Fukada, H., Mikami, S. et al. (2000) Isolation and characterization of phytase isozymes produced by Aspergillus oryzae. Biotechnology Letters 22, 1797-1802.
    • (2000) Biotechnology Letters , vol.22 , pp. 1797-1802
    • Fujita, J.1    Budda, N.2    Tujimoto, M.3    Yamane, Y.4    Fukada, H.5    Mikami, S.6
  • 32
    • 1842525539 scopus 로고    scopus 로고
    • Enhancing the thermal tolerance and gastric performance of a microbial phytase for use as a phosphate-mobilizing monogastric-feed supplement
    • Garrett, J.B., Kretz, K.A., O'Donoghue, E., Kerovuo, J., Kim, W., Barton, N.R. et al. (2004) Enhancing the thermal tolerance and gastric performance of a microbial phytase for use as a phosphate-mobilizing monogastric-feed supplement. Applied and Environmental Microbiology 70, 3041-3046.
    • (2004) Applied and Environmental Microbiology , vol.70 , pp. 3041-3046
    • Garrett, J.B.1    Kretz, K.A.2    O'Donoghue, E.3    Kerovuo, J.4    Kim, W.5    Barton, N.R.6
  • 33
    • 1542442162 scopus 로고    scopus 로고
    • Effectiveness of an experimental consensus phytase in improving dietary phytate-phosphorus utilization by weanling pigs
    • Gentile, J.M., Ronecker, K.R., Crowe, S.E., Pond, W.G. and Lei, X.G. (2003) Effectiveness of an experimental consensus phytase in improving dietary phytate-phosphorus utilization by weanling pigs. Journal of Animal Science 81, 2751-2757.
    • (2003) Journal of Animal Science , vol.81 , pp. 2751-2757
    • Gentile, J.M.1    Ronecker, K.R.2    Crowe, S.E.3    Pond, W.G.4    Lei, X.G.5
  • 34
    • 0023957340 scopus 로고
    • Purification and characterization of phytase from cotyledons of germinating soybean seeds
    • Gibson, D.M. and Ullah, A.H.J. (1988) Purification and characterization of phytase from cotyledons of germinating soybean seeds. Archives of Biochemistry and Biophysics 260, 503-513.
    • (1988) Archives of Biochemistry and Biophysics , vol.260 , pp. 503-513
    • Gibson, D.M.1    Ullah, A.H.J.2
  • 35
    • 0033952605 scopus 로고    scopus 로고
    • Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities
    • Golovan, S., Wang, G., Zhang, J. and Forsberg, C.W. (2000) Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities. Canadian Journal of Microbiology 46, 59-71.
    • (2000) Canadian Journal of Microbiology , vol.46 , pp. 59-71
    • Golovan, S.1    Wang, G.2    Zhang, J.3    Forsberg, C.W.4
  • 37
    • 0037032234 scopus 로고    scopus 로고
    • Purification and characterization of three phytases from germinated lupine seeds (Lupinus albus var. Amiga)
    • Greiner, R. (2002) Purification and characterization of three phytases from germinated lupine seeds (Lupinus albus var. Amiga). Journal of Agricultural and Food Chemistry 50, 6858-6864.
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 6858-6864
    • Greiner, R.1
  • 38
    • 16844386691 scopus 로고    scopus 로고
    • Purification and properties of a phytate-degrading enzyme from Pantoea agglomerans
    • Greiner, R. (2004a) Purification and properties of a phytate-degrading enzyme from Pantoea agglomerans. The Protein Journal 23, 567-576.
    • (2004) The Protein Journal , vol.23 , pp. 567-576
    • Greiner, R.1
  • 39
    • 16844371242 scopus 로고    scopus 로고
    • Degradation of myo-inositol hexakisphosphate by a phytate-degrading enzyme from Pantoea agglomerans
    • Greiner, R. (2004b) Degradation of myo-inositol hexakisphosphate by a phytate-degrading enzyme from Pantoea agglomerans. The Protein Journal 23, 577-585.
    • (2004) The Protein Journal , vol.23 , pp. 577-585
    • Greiner, R.1
  • 40
    • 84890773965 scopus 로고    scopus 로고
    • Phytate-degrading enzymes: regulation of synthesis in microorganisms and plants
    • In: Turner, B.L., Richardson, A.E. and Mullaney, E.J. (eds), CAB International, Wallingford, UK,
    • Greiner, R. (2006) Phytate-degrading enzymes: regulation of synthesis in microorganisms and plants. In: Turner, B.L., Richardson, A.E. and Mullaney, E.J. (eds) Inositol Phosphates: Linking Agriculture and Environment. CAB International, Wallingford, UK, pp. 78-96.
    • (2006) Inositol Phosphates: Linking Agriculture and Environment , pp. 78-96
    • Greiner, R.1
  • 41
    • 33749861588 scopus 로고    scopus 로고
    • myo-Inositol phosphate isomers generated by the action of a phytate-degrading enzyme from Klebsiella terrigena upon phytate
    • Greiner, R. and Carlsson, N.G. (2006) myo-Inositol phosphate isomers generated by the action of a phytate-degrading enzyme from Klebsiella terrigena upon phytate. Canadian Journal of Microbiology 52, 759-768.
    • (2006) Canadian Journal of Microbiology , vol.52 , pp. 759-768
    • Greiner, R.1    Carlsson, N.G.2
  • 42
    • 35348867955 scopus 로고    scopus 로고
    • Purification and characterisation of a bacterial phytase whose outstanding properties make it exceptionally useful as a feed supplement
    • Greiner, R. and Farouk, A. (2007) Purification and characterisation of a bacterial phytase whose outstanding properties make it exceptionally useful as a feed supplement. The Protein Journal 26, 467-474.
    • (2007) The Protein Journal , vol.26 , pp. 467-474
    • Greiner, R.1    Farouk, A.2
  • 44
    • 0345493850 scopus 로고    scopus 로고
    • Purification and characterization of a phytatedegrading enzyme from germinated oat (Avena sativa)
    • Greiner, R. and Larsson Alminger, M. (1999) Purification and characterization of a phytatedegrading enzyme from germinated oat (Avena sativa). Journal of the Science of Food and Agriculture 79, 1453-1460.
    • (1999) Journal of the Science of Food and Agriculture , vol.79 , pp. 1453-1460
    • Greiner, R.1    Larsson Alminger, M.2
  • 45
    • 0035533231 scopus 로고    scopus 로고
    • Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by phytate-degrading enzymes of cereals
    • Greiner, R. and Larsson Alminger, M. (2001) Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by phytate-degrading enzymes of cereals. Journal of Food Biochemistry 25, 229-248.
    • (2001) Journal of Food Biochemistry , vol.25 , pp. 229-248
    • Greiner, R.1    Larsson Alminger, M.2
  • 49
    • 0034681025 scopus 로고    scopus 로고
    • Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of Escherichia coli
    • Greiner, R., Carlsson, N.G. and Larsson Alminger, M. (2000a) Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of Escherichia coli. Journal of Biotechnology 84, 53-62.
    • (2000) Journal of Biotechnology , vol.84 , pp. 53-62
    • Greiner, R.1    Carlsson, N.G.2    Larsson Alminger, M.3
  • 50
    • 0033846612 scopus 로고    scopus 로고
    • Identification and properties of myoinositol hexakisphosphate phosphohydrolases (phytases) from barley (Hordeum vulgare)
    • Greiner, R., Jany, K.-D. and Larsson Alminger, M. (2000b) Identification and properties of myoinositol hexakisphosphate phosphohydrolases (phytases) from barley (Hordeum vulgare). Journal of Cereal Science 31, 127-139.
    • (2000) Journal of Cereal Science , vol.31 , pp. 127-139
    • Greiner, R.1    Jany, K.-D.2    Larsson Alminger, M.3
  • 51
    • 17944362173 scopus 로고    scopus 로고
    • Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of baker's yeast
    • Greiner, R., Larsson Alminger, M. and Carlsson, N.G. (2001a) Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of baker's yeast. Journal of Agricultural and Food Chemistry 49, 2228-2233.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 2228-2233
    • Greiner, R.1    Larsson Alminger, M.2    Carlsson, N.G.3
  • 55
    • 35948974760 scopus 로고    scopus 로고
    • myo-Inositol phosphate isomers generated by the action of a phytase from a Malaysian waste-water bacterium
    • Greiner, R., Farouk, A., Carlsson, N.-G. and Konietzny U. (2007a) myo-Inositol phosphate isomers generated by the action of a phytase from a Malaysian waste-water bacterium. The Protein Journal 26, 577-584.
    • (2007) The Protein Journal , vol.26 , pp. 577-584
    • Greiner, R.1    Farouk, A.2    Carlsson, N.-G.3    Konietzny, U.4
  • 56
    • 34347382434 scopus 로고    scopus 로고
    • Pathway of phytate dephosphorylation by ß-propeller phytases of different origin
    • Greiner, R., Lim, B.L., Cheng, C. and Carlsson, N.G. (2007b) Pathway of phytate dephosphorylation by ß-propeller phytases of different origin. Canadian Journal of Microbiology 53, 488-495.
    • (2007) Canadian Journal of Microbiology , vol.53 , pp. 488-495
    • Greiner, R.1    Lim, B.L.2    Cheng, C.3    Carlsson, N.G.4
  • 57
    • 70350142630 scopus 로고    scopus 로고
    • Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9
    • Brazilian Journal of Microbiology
    • Greiner, R., Gomes da Silva, L. and Couri S. (2009) Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9. Brazilian Journal of Microbiology 40.
    • (2009) , vol.40
    • Greiner, R.1    Gomes Da Silva, L.2    Couri, S.3
  • 58
    • 0033950597 scopus 로고    scopus 로고
    • Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded state
    • Ha, N.C., Oh, B.C., Shin, S., Kim, H.J., Oh, T.K., Kim, Y.O. et al. (2000) Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded state. Nature Structural Biology 7, 147-153.
    • (2000) Nature Structural Biology , vol.7 , pp. 147-153
    • Ha, N.C.1    Oh, B.C.2    Shin, S.3    Kim, H.J.4    Oh, T.K.5    Kim, Y.O.6
  • 61
    • 84954882595 scopus 로고
    • Myo-inositol polyphosphate intermediates in the dephosphorylation of phytic acid by acid phosphatase with phytase activity from rice bran
    • Hayakawa, T., Suzuki, K., Miura, H., Ohno, T. and Igaue, I. (1990) Myo-inositol polyphosphate intermediates in the dephosphorylation of phytic acid by acid phosphatase with phytase activity from rice bran. Agricultural and Biological Chemistry 54, 279-286.
    • (1990) Agricultural and Biological Chemistry , vol.54 , pp. 279-286
    • Hayakawa, T.1    Suzuki, K.2    Miura, H.3    Ohno, T.4    Igaue, I.5
  • 62
    • 0034869290 scopus 로고    scopus 로고
    • A novel phytase with sequence similarity to purple acid phosphatase is expressed in cotyledons of germinating soybean seedling
    • Hegeman, C.E. and Grabau, E.A. (2001) A novel phytase with sequence similarity to purple acid phosphatase is expressed in cotyledons of germinating soybean seedling. Plant Physiology 126, 1598-1608.
    • (2001) Plant Physiology , vol.126 , pp. 1598-1608
    • Hegeman, C.E.1    Grabau, E.A.2
  • 64
    • 0029892463 scopus 로고    scopus 로고
    • Hydrolysis of phytate and inositol tri-, tetra-, and pentaphosphates by the intestinal mucosa of the pig
    • Hu, H.L., Wise, A. and Henderson, C. (1996) Hydrolysis of phytate and inositol tri-, tetra-, and pentaphosphates by the intestinal mucosa of the pig. Nutrition Research 16, 781-787.
    • (1996) Nutrition Research , vol.16 , pp. 781-787
    • Hu, H.L.1    Wise, A.2    Henderson, C.3
  • 65
    • 50249156831 scopus 로고    scopus 로고
    • A novel phytase from Yersinia rhodei with high phytate hydrolysis activity under low pH and strong pepsin conditions
    • Huang, H., Luo, H., Wang, Y., Fu, D., Shao, N., Wang, G. et al. (2008). A novel phytase from Yersinia rhodei with high phytate hydrolysis activity under low pH and strong pepsin conditions. Applied Microbiology and Biotechnology 80, 417-426.
    • (2008) Applied Microbiology and Biotechnology , vol.80 , pp. 417-426
    • Huang, H.1    Luo, H.2    Wang, Y.3    Fu, D.4    Shao, N.5    Wang, G.6
  • 66
    • 0030478075 scopus 로고    scopus 로고
    • Maize root phytase
    • Hübel, F. and Beck, E. (1996) Maize root phytase. Plant Physiology 112, 1429-1436.
    • (1996) Plant Physiology , vol.112 , pp. 1429-1436
    • Hübel, F.1    Beck, E.2
  • 68
    • 0027935658 scopus 로고
    • Phytase activity in the human and rat small intestine
    • Iqbal, T.H., Lewis, K.O. and Cooper, B.T. (1994) Phytase activity in the human and rat small intestine. Gut 35, 1233-1236.
    • (1994) Gut , vol.35 , pp. 1233-1236
    • Iqbal, T.H.1    Lewis, K.O.2    Cooper, B.T.3
  • 70
    • 0026846841 scopus 로고
    • The effect of supplementary Aspergillus niger phytase in diets for pigs on concentration and apparent digestibility of dry matter,total phosphorus, and phytic acid in different sections of the alimentary tract
    • Jongbloed, A.W., Mroz, Z. and Kemme, P.A. (1992) The effect of supplementary Aspergillus niger phytase in diets for pigs on concentration and apparent digestibility of dry matter,total phosphorus, and phytic acid in different sections of the alimentary tract. Journal of Animal Science 70, 1159-1168.
    • (1992) Journal of Animal Science , vol.70 , pp. 1159-1168
    • Jongbloed, A.W.1    Mroz, Z.2    Kemme, P.A.3
  • 71
    • 0031747416 scopus 로고    scopus 로고
    • Isolation, characterization, molecular gene cloning and sequencing of a novel phytase from Bacillus subtilis
    • Kerovuo, J., Lauraeus, M., Nurminen, P., Kalkinnen, N. and Apajalahti, J. (1998) Isolation, characterization, molecular gene cloning and sequencing of a novel phytase from Bacillus subtilis. Applied and Environmental Microbiology 64, 2079-2085.
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 2079-2085
    • Kerovuo, J.1    Lauraeus, M.2    Nurminen, P.3    Kalkinnen, N.4    Apajalahti, J.5
  • 73
    • 0033369153 scopus 로고    scopus 로고
    • Culture conditions for a new phytase-producing fungus
    • Kim, D.-S., Godber, J.S. and Kim, H.-R. (1999) Culture conditions for a new phytase-producing fungus. Biotechnology Letters 21, 1077-1081.
    • (1999) Biotechnology Letters , vol.21 , pp. 1077-1081
    • Kim, D.-S.1    Godber, J.S.2    Kim, H.-R.3
  • 74
    • 0041854630 scopus 로고    scopus 로고
    • Isolation and characterization of a phytase with improved properties from Citrobacter braakii
    • Kim, H.W., Kim, Y.O., Lee, J.H., Kim, K.K. and. Kim, Y.J. (2003) Isolation and characterization of a phytase with improved properties from Citrobacter braakii. Biotechnology Letters 25, 1231-1234.
    • (2003) Biotechnology Letters , vol.25 , pp. 1231-1234
    • Kim, H.W.1    Kim, Y.O.2    Lee, J.H.3    Kim, K.K.4    Kim, Y.J.5
  • 75
    • 42149088826 scopus 로고    scopus 로고
    • Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR
    • Kim, M.-S. and Lei X.G. (2008) Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR. Applied Microbiology and Biotechnology 79, 69-75.
    • (2008) Applied Microbiology and Biotechnology , vol.79 , pp. 69-75
    • Kim, M.-S.1    Lei, X.G.2
  • 76
    • 33745159981 scopus 로고    scopus 로고
    • Shifting the pH profile of Aspergillus niger phyA phytase to match the stomach pH enhances its effectiveness as an animal feed additive
    • Kim, T., Mullaney, E.J., Porres, J.M., Roneker, K.R., Crowe, S., Rice, S. et al. (2006) Shifting the pH profile of Aspergillus niger phyA phytase to match the stomach pH enhances its effectiveness as an animal feed additive. Applied and Environmental Microbiology 72, 4397-4403.
    • (2006) Applied and Environmental Microbiology , vol.72 , pp. 4397-4403
    • Kim, T.1    Mullaney, E.J.2    Porres, J.M.3    Roneker, K.R.4    Crowe, S.5    Rice, S.6
  • 78
    • 0032080595 scopus 로고    scopus 로고
    • Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and its overexpression in Escherichia coli.
    • Kim, Y.-O., Lee, J.-K., Kim, H.-K., Yu, J.-H. and Oh, T.-K. (1998b) Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and its overexpression in Escherichia coli. FEMS Microbiology Letters 162, 185-191.
    • (1998) FEMS Microbiology Letters , vol.162 , pp. 185-191
    • Kim, Y.-O.1    Lee, J.-K.2    Kim, H.-K.3    Yu, J.-H.4    Oh, T.-K.5
  • 80
    • 19944373812 scopus 로고    scopus 로고
    • Bacterial phytase: potential application, in vivo function and regulation of its synthesis
    • Konietzny, U. and Greiner, R. (2004) Bacterial phytase: potential application, in vivo function and regulation of its synthesis. Brazilian Journal of Microbiology 35, 11-18.
    • (2004) Brazilian Journal of Microbiology , vol.35 , pp. 11-18
    • Konietzny, U.1    Greiner, R.2
  • 83
    • 0027443426 scopus 로고
    • Purification and characterization of phytase (myo-inositol hexakisphosphate phosphohydrolase) accumulated in maize (Zea mays) seedlings during germination
    • Laboure, A.M., Gagnon, J. and Lescure, A.M. (1993) Purification and characterization of phytase (myo-inositol hexakisphosphate phosphohydrolase) accumulated in maize (Zea mays) seedlings during germination. Biochemical Journal 295, 503-513.
    • (1993) Biochemical Journal , vol.295 , pp. 503-513
    • Laboure, A.M.1    Gagnon, J.2    Lescure, A.M.3
  • 84
    • 0027193329 scopus 로고
    • Influence of culture conditions on the biosynthesis of Schwanniomyces castellii phytase
    • Lambrechts, C., Boze, H., Segueilha, L., Moulin, G. and Galzy, P. (1993) Influence of culture conditions on the biosynthesis of Schwanniomyces castellii phytase. Biotechnology Letters 15, 399-404.
    • (1993) Biotechnology Letters , vol.15 , pp. 399-404
    • Lambrechts, C.1    Boze, H.2    Segueilha, L.3    Moulin, G.4    Galzy, P.5
  • 85
    • 85047683976 scopus 로고    scopus 로고
    • Expression, gene cloning, and characterization of five novel phytases from four basidiomycete fungi: Peniophora lycii, Agrocybe pediades, a Ceriporia sp., and Trametes pubescens
    • Lassen, S.F., Breinholt, J., Ostergaard, P.R., Brugger, R., Bischoff, A., Wyss, M. et al. (2001) Expression, gene cloning, and characterization of five novel phytases from four basidiomycete fungi: Peniophora lycii, Agrocybe pediades, a Ceriporia sp., and Trametes pubescens. Applied and Environmental Microbiology 67, 4701-4707.
    • (2001) Applied and Environmental Microbiology , vol.67 , pp. 4701-4707
    • Lassen, S.F.1    Breinholt, J.2    Ostergaard, P.R.3    Brugger, R.4    Bischoff, A.5    Wyss, M.6
  • 86
    • 0033769666 scopus 로고    scopus 로고
    • Exchanging the active site between phytases for altering the functional properties of the enzyme
    • Lehmann, M., Lopez-Ulibarri, R., Loch, C., Viarouge, C., Wyss, M. and van Loon A.P.G.M. (2000) Exchanging the active site between phytases for altering the functional properties of the enzyme. Protein Science 9, 1866-1872.
    • (2000) Protein Science , vol.9 , pp. 1866-1872
    • Lehmann, M.1    Lopez-Ulibarri, R.2    Loch, C.3    Viarouge, C.4    Wyss, M.5    Van Loon, A.P.G.M.6
  • 87
    • 0036271498 scopus 로고    scopus 로고
    • The consensus concept for thermostability engineering of proteins: further proof of concept
    • Lehmann, M., Loch, C., Middendorf, A., Studer, D., Lassen, S.F., Pasamontes, L. et al. (2002) The consensus concept for thermostability engineering of proteins: further proof of concept. Protein Engineering 15, 403-411.
    • (2002) Protein Engineering , vol.15 , pp. 403-411
    • Lehmann, M.1    Loch, C.2    Middendorf, A.3    Studer, D.4    Lassen, S.F.5    Pasamontes, L.6
  • 88
    • 0345393313 scopus 로고    scopus 로고
    • Phytase enzymology, applications, and biotechnology
    • Lei, X.G. and Porres J. (2003) Phytase enzymology, applications, and biotechnology. Biotechnology Letters 25, 1787-1794.
    • (2003) Biotechnology Letters , vol.25 , pp. 1787-1794
    • Lei, X.G.1    Porres, J.2
  • 89
    • 0034767777 scopus 로고    scopus 로고
    • Biotechnological development of effective phytases for mineral nutrition and environmental protection
    • Lei, X.G. and Stahl, C.H. (2001) Biotechnological development of effective phytases for mineral nutrition and environmental protection. Applied Microbiology and Biotechnology 57, 478-481.
    • (2001) Applied Microbiology and Biotechnology , vol.57 , pp. 478-481
    • Lei, X.G.1    Stahl, C.H.2
  • 90
    • 0027273836 scopus 로고
    • Supplemental microbial phytase improves bioavailability of dietary zinc to weanling pigs
    • Lei, X.G., Ku, P.K., Miller, E.R., Ullrey, D.E. and Yokoyama, M.T. (1993) Supplemental microbial phytase improves bioavailability of dietary zinc to weanling pigs. Journal of Nutrition 123, 1117-1123.
    • (1993) Journal of Nutrition , vol.123 , pp. 1117-1123
    • Lei, X.G.1    Ku, P.K.2    Miller, E.R.3    Ullrey, D.E.4    Yokoyama, M.T.5
  • 91
    • 0030916045 scopus 로고    scopus 로고
    • Purification and characterization of phytase induced in tomato roots under phosphorus-deficient conditions
    • Li, M., Osaki, M., Honma, M. and Tadano, T. (1997) Purification and characterization of phytase induced in tomato roots under phosphorus-deficient conditions. Soil Science and Plant Nutrition 43, 179-190.
    • (1997) Soil Science and Plant Nutrition , vol.43 , pp. 179-190
    • Li, M.1    Osaki, M.2    Honma, M.3    Tadano, T.4
  • 92
    • 34547768136 scopus 로고    scopus 로고
    • Distribution and diversity of phytatemineralizing bacteria
    • Lim, B.L., Yeung, P., Cheng, C. and Hill, J.E. (2007) Distribution and diversity of phytatemineralizing bacteria. The ISME Journal 1, 321-330.
    • (2007) The ISME Journal , vol.1 , pp. 321-330
    • Lim, B.L.1    Yeung, P.2    Cheng, C.3    Hill, J.E.4
  • 93
    • 0033952704 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli phytase and its complex with phytate
    • Lim, D., Golovan, S., Forsberg, C.W. and Jia, Z. (2000) Crystal structure of Escherichia coli phytase and its complex with phytate. Nature Structural Biology 7, 108-113.
    • (2000) Nature Structural Biology , vol.7 , pp. 108-113
    • Lim, D.1    Golovan, S.2    Forsberg, C.W.3    Jia, Z.4
  • 94
    • 0015921511 scopus 로고
    • The phytases: II. Properties of phytase fraction F1 and F2 from wheat bran and the myo-inositol phosphates produced by fraction F2.
    • Lim, P.E. and Tate, M.E. (1973) The phytases: II. Properties of phytase fraction F1 and F2 from wheat bran and the myo-inositol phosphates produced by fraction F2. Biochimica et Biophysica Acta 302, 326-328.
    • (1973) Biochimica et Biophysica Acta , vol.302 , pp. 326-328
    • Lim, P.E.1    Tate, M.E.2
  • 95
    • 0028262202 scopus 로고
    • Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.
    • Lindqvist, Y., Schneider, G. and Vihko, P. (1994) Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism. European Journal of Biochemistry 221, 129-142.
    • (1994) European Journal of Biochemistry , vol.221 , pp. 129-142
    • Lindqvist, Y.1    Schneider, G.2    Vihko, P.3
  • 96
    • 0001501029 scopus 로고
    • Isolation, purification and characterization of phytase from germinating mung beans
    • Mandel, N.C., Burman, S. and Biswas, B.B. (1972) Isolation, purification and characterization of phytase from germinating mung beans. Phytochemistry 11, 495-502.
    • (1972) Phytochemistry , vol.11 , pp. 495-502
    • Mandel, N.C.1    Burman, S.2    Biswas, B.B.3
  • 97
    • 0033083360 scopus 로고    scopus 로고
    • Structure of two maize phytase genes and their spatio-temporal expression during seedling development
    • Maugenest, S., Martinez, I., Godin, B., Perez, P. and Lescure, A.-M. (1999) Structure of two maize phytase genes and their spatio-temporal expression during seedling development. Plant Molecular Biology 39, 502-514.
    • (1999) Plant Molecular Biology , vol.39 , pp. 502-514
    • Maugenest, S.1    Martinez, I.2    Godin, B.3    Perez, P.4    Lescure, A.-M.5
  • 98
    • 0033526419 scopus 로고    scopus 로고
    • An expression system matures: a highly efficient and cost-effective process for phytase production by recombinant strains of Hansenula polymorpha
    • Mayer, A.F., Hellmuth, K., Schlieker, H., Lopez-Ulibarri, R., Oertel, S., Dahlems, U. et al. (1999) An expression system matures: a highly efficient and cost-effective process for phytase production by recombinant strains of Hansenula polymorpha. Biotechnology and Bioengineering 63, 373-381.
    • (1999) Biotechnology and Bioengineering , vol.63 , pp. 373-381
    • Mayer, A.F.1    Hellmuth, K.2    Schlieker, H.3    Lopez-Ulibarri, R.4    Oertel, S.5    Dahlems, U.6
  • 99
    • 33747879395 scopus 로고    scopus 로고
    • Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase
    • Mehta, B.D., Jog, S.P., Johnson, S.C. and Murthy, P.P.N. (2006) Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase. Phytochemistry 67, 1874-1886.
    • (2006) Phytochemistry , vol.67 , pp. 1874-1886
    • Mehta, B.D.1    Jog, S.P.2    Johnson, S.C.3    Murthy, P.P.N.4
  • 100
    • 0036383441 scopus 로고    scopus 로고
    • Overexpression of the phytase from Escherichia coli and its extracellular production in bioreactors
    • Miksch, G., Kleist, S., Friehs, K. and Flaschel, E. (2002) Overexpression of the phytase from Escherichia coli and its extracellular production in bioreactors. Applied Microbiology and Biotechnology 59, 685-694.
    • (2002) Applied Microbiology and Biotechnology , vol.59 , pp. 685-694
    • Miksch, G.1    Kleist, S.2    Friehs, K.3    Flaschel, E.4
  • 101
    • 0031034203 scopus 로고    scopus 로고
    • The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila
    • Mitchell, D.B., Vogel, K., Weimann, B.J., Pasamontes, L. and van Loon, A.P.G.M. (1997) The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila. Microbiology 143, 245-252.
    • (1997) Microbiology , vol.143 , pp. 245-252
    • Mitchell, D.B.1    Vogel, K.2    Weimann, B.J.3    Pasamontes, L.4    Van Loon, A.P.G.M.5
  • 106
    • 84986777972 scopus 로고
    • Production of phytase by Aspergillus ficuum and reduction of phytic acid content in canola meal
    • Nair, V.C., Laflamme, J. and Duvnjak, Z. (1991) Production of phytase by Aspergillus ficuum and reduction of phytic acid content in canola meal. Journal of the Science of Food and Agriculture 54, 355-365.
    • (1991) Journal of the Science of Food and Agriculture , vol.54 , pp. 355-365
    • Nair, V.C.1    Laflamme, J.2    Duvnjak, Z.3
  • 107
    • 0005204272 scopus 로고    scopus 로고
    • Purification and characterization of phytase from bran of Triticum aestivum L.cv. Nourin#61
    • Nakano, T., Joh, T., Tokumoto, E. and Hayakawa, T. (1999) Purification and characterization of phytase from bran of Triticum aestivum L. cv. Nourin#61. Food Science and Technology Research 5, 18-23.
    • (1999) Food Science and Technology Research , vol.5 , pp. 18-23
    • Nakano, T.1    Joh, T.2    Tokumoto, E.3    Hayakawa, T.4
  • 108
    • 0034180451 scopus 로고    scopus 로고
    • The pathway of dephosphorylation of myo-inositol hexakisphosphate by phytases from wheat bran of Triticum aestivum L.cv. Nourin#61.
    • Nakano, T., Joh, T., Narita, K. and Hayakawa, T. (2000) The pathway of dephosphorylation of myo-inositol hexakisphosphate by phytases from wheat bran of Triticum aestivum L. cv. Nourin#61. Bioscience, Biotechnology and Biochemistry 64, 995-1003.
    • (2000) Bioscience, Biotechnology and Biochemistry , vol.64 , pp. 995-1003
    • Nakano, T.1    Joh, T.2    Narita, K.3    Hayakawa, T.4
  • 110
    • 0035859795 scopus 로고    scopus 로고
    • Calcium-dependent catalytic activity of a novel phytase from Bacillus amyloliquefaciens DS11
    • Oh, B.C., Chang, B.S., Park, K.H., Ha, N.C., Kim, H.K. et al. (2001) Calcium-dependent catalytic activity of a novel phytase from Bacillus amyloliquefaciens DS11. Biochemistry 40, 9669-9676.
    • (2001) Biochemistry , vol.40 , pp. 9669-9676
    • Oh, B.C.1    Chang, B.S.2    Park, K.H.3    Ha, N.C.4    Kim, H.K.5
  • 112
    • 0033228316 scopus 로고    scopus 로고
    • Comparative enzymatic hydrolysis of phytate in various animal feedstuffs with two different phytases
    • Park, S.C., Choi, Y.W. and Oh, T.K. (1999) Comparative enzymatic hydrolysis of phytate in various animal feedstuffs with two different phytases. Journal of Veterinary Medical Science 61, 1257-1259.
    • (1999) Journal of Veterinary Medical Science , vol.61 , pp. 1257-1259
    • Park, S.C.1    Choi, Y.W.2    Oh, T.K.3
  • 114
    • 0030898612 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus
    • Pasamontes, L., Haiker, M., Wyss, M., Tessier, M. and Loon A.P.G.M. (1997b) Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus. Applied and Environmental Microbiology 63, 1696-1700.
    • (1997) Applied and Environmental Microbiology , vol.63 , pp. 1696-1700
    • Pasamontes, L.1    Haiker, M.2    Wyss, M.3    Tessier, M.4    Loon, A.P.G.M.5
  • 116
    • 0034989016 scopus 로고    scopus 로고
    • Microbial phytase does not improve protein-amino acid utilization in soybean meal fed to young chickens
    • Peter, C.M. and Baker, D.H. (2001) Microbial phytase does not improve protein-amino acid utilization in soybean meal fed to young chickens. Journal of Nutrition 131, 1792-1797.
    • (2001) Journal of Nutrition , vol.131 , pp. 1792-1797
    • Peter, C.M.1    Baker, D.H.2
  • 117
    • 0032964364 scopus 로고    scopus 로고
    • Susceptibility of wheat and Aspergillus niger phytases to inactivation by gastrointestinal enzymes
    • Phillippy, B.Q. (1999) Susceptibility of wheat and Aspergillus niger phytases to inactivation by gastrointestinal enzymes. Journal of Agricultural and Food Chemistry 47, 1385-1388.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 1385-1388
    • Phillippy, B.Q.1
  • 118
    • 0001359513 scopus 로고
    • Phytate phosphorus utilization and intestinal phosphatases in pigs fed low phosphorus wheat or corn diets
    • Pointillart, A., Fontaine, N. and Thomasset, M. (1984) Phytate phosphorus utilization and intestinal phosphatases in pigs fed low phosphorus wheat or corn diets. Nutrition Reports International 22, 473-483.
    • (1984) Nutrition Reports International , vol.22 , pp. 473-483
    • Pointillart, A.1    Fontaine, N.2    Thomasset, M.3
  • 119
    • 0021884626 scopus 로고
    • Phosphorus utilization, intestinal phosphatases and hormonal control of calcium metabolism in pigs fed phytic phosphorus: soyabean or rapeseed diets
    • Pointillart, A., Fontaine, N., Thomasset, M. and Jay, M.E. (1985) Phosphorus utilization, intestinal phosphatases and hormonal control of calcium metabolism in pigs fed phytic phosphorus: soyabean or rapeseed diets. Nutrition Reports International 32, 155-167.
    • (1985) Nutrition Reports International , vol.32 , pp. 155-167
    • Pointillart, A.1    Fontaine, N.2    Thomasset, M.3    Jay, M.E.4
  • 120
    • 0028128764 scopus 로고
    • Site-directed mutagenesis of prostatic acid phosphatase. Catalytically important aspartic acid 258, substrate specificity, and oligomerization
    • Porvari, K.S., Herrala, A.M., Kurkela, R.M., Taavitsainen, P.A., Lindqvist, Y., Schneider, G. et al. (1994) Site-directed mutagenesis of prostatic acid phosphatase. Catalytically important aspartic acid 258, substrate specificity, and oligomerization. Journal of Biological Chemistry 269, 22642-22646.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 22642-22646
    • Porvari, K.S.1    Herrala, A.M.2    Kurkela, R.M.3    Taavitsainen, P.A.4    Lindqvist, Y.5    Schneider, G.6
  • 121
    • 0020458827 scopus 로고
    • Purification and properties of phytate-specific phosphatase from Bacillus subtilis
    • Powar, V.K. and Jagannathan, V. (1982) Purification and properties of phytate-specific phosphatase from Bacillus subtilis. Journal of Bacteriology 151, 1102-1108.
    • (1982) Journal of Bacteriology , vol.151 , pp. 1102-1108
    • Powar, V.K.1    Jagannathan, V.2
  • 122
    • 34250815835 scopus 로고    scopus 로고
    • Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myoinositol polyphosphatase
    • Puhl, A.A., Gruninger, R.J., Greiner, R., Janzen, T.W., Mosimann, S.C. and Selinger, L.B. (2007) Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myoinositol polyphosphatase. Protein Science 16, 1368-1378.
    • (2007) Protein Science , vol.16 , pp. 1368-1378
    • Puhl, A.A.1    Gruninger, R.J.2    Greiner, R.3    Janzen, T.W.4    Mosimann, S.C.5    Selinger, L.B.6
  • 123
    • 49249114927 scopus 로고    scopus 로고
    • Kinetics, substrate specificity, and stereospecificity of two new protein tyrosine phosphatase-like inositol polyphosphatases from Selenomonas lacticifex
    • Puhl, A.A., Greiner, R. and Selinger, L.B. (2008a) Kinetics, substrate specificity, and stereospecificity of two new protein tyrosine phosphatase-like inositol polyphosphatases from Selenomonas lacticifex. Biochemistry and Cell Biology 86, 322-330.
    • (2008) Biochemistry and Cell Biology , vol.86 , pp. 322-330
    • Puhl, A.A.1    Greiner, R.2    Selinger, L.B.3
  • 124
    • 48949117581 scopus 로고    scopus 로고
    • A protein tyrosine phosphatase-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica has specificity for the 5-phosphate of myo-inositol hexakisphosphate.
    • Puhl, A.A., Greiner, R. and Selinger, L.B. (2008b) A protein tyrosine phosphatase-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica has specificity for the 5-phosphate of myo-inositol hexakisphosphate. International Journal of Biochemistry and Cell Biology 40, 2053-2064.
    • (2008) International Journal of Biochemistry and Cell Biology , vol.40 , pp. 2053-2064
    • Puhl, A.A.1    Greiner, R.2    Selinger, L.B.3
  • 125
    • 58549085955 scopus 로고    scopus 로고
    • Stereospecificity of myo-inositol hexakisphosphate hydrolysis by a protein tyrosine phosphatase-like inositol polyphosphatase from Megasphaera elsdenii
    • Puhl, A.A., Greiner, R. and Selinger, L.B. (2009) Stereospecificity of myo-inositol hexakisphosphate hydrolysis by a protein tyrosine phosphatase-like inositol polyphosphatase from Megasphaera elsdenii. Applied Microbiology and Biotechnology 82, 95-103.
    • (2009) Applied Microbiology and Biotechnology , vol.82 , pp. 95-103
    • Puhl, A.A.1    Greiner, R.2    Selinger, L.B.3
  • 127
  • 128
    • 34848887963 scopus 로고    scopus 로고
    • Polynucleotides encoding phytase polypeptides
    • US Patent 7186817
    • Rasmussen, S.K., Johansen, K.S. and Sørensen, M.B. (2007) Polynucleotides encoding phytase polypeptides. US Patent 7186817.
    • (2007)
    • Rasmussen, S.K.1    Johansen, K.S.2    Sørensen, M.B.3
  • 129
    • 0033562103 scopus 로고    scopus 로고
    • Different sensitivity of recombinant Aspergillus niger phytase (r-phyA) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro
    • Rodriguez, E., Porres, J.M., Han, Y. and Lei X.G. (1999) Different sensitivity of recombinant Aspergillus niger phytase (r-phyA) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro. Archives of Biochemistry and Biophysics 365, 262-267.
    • (1999) Archives of Biochemistry and Biophysics , vol.365 , pp. 262-267
    • Rodriguez, E.1    Porres, J.M.2    Han, Y.3    Lei, X.G.4
  • 130
    • 0034673345 scopus 로고    scopus 로고
    • Expression of the Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme
    • Rodriguez, E., Mullaney, E.J. and Lei, X.G. (2000) Expression of the Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme. Biochemical and Biophysical Research Communications 268, 373-378.
    • (2000) Biochemical and Biophysical Research Communications , vol.268 , pp. 373-378
    • Rodriguez, E.1    Mullaney, E.J.2    Lei, X.G.3
  • 131
    • 0034732993 scopus 로고    scopus 로고
    • Identification of mammalian-like purple acid phosphatases in a wide range of plants
    • Schenk, G., Guddat, L.W., Ge, Y., Carrington, L.E., Hume, D.A., Hamilton, J. et al. (2000) Identification of mammalian-like purple acid phosphatases in a wide range of plants. Gene 250, 117-125.
    • (2000) Gene , vol.250 , pp. 117-125
    • Schenk, G.1    Guddat, L.W.2    Ge, Y.3    Carrington, L.E.4    Hume, D.A.5    Hamilton, J.6
  • 132
    • 0000482376 scopus 로고
    • Alkaline phytase activity in nonionic detergent extracts of legume seeds
    • Scott, J.J. (1991) Alkaline phytase activity in nonionic detergent extracts of legume seeds. Plant Physiology 95, 1298-1301.
    • (1991) Plant Physiology , vol.95 , pp. 1298-1301
    • Scott, J.J.1
  • 133
    • 0347167238 scopus 로고    scopus 로고
    • Implications of phytic acid and supplemental microbial phytase in poultry nutrition: a review
    • Sebastian, S., Touchburn, S.P. and Chavez, E.R. (1998) Implications of phytic acid and supplemental microbial phytase in poultry nutrition: a review. World's Poultry Science Journal 54, 27-47.
    • (1998) World's Poultry Science Journal , vol.54 , pp. 27-47
    • Sebastian, S.1    Touchburn, S.P.2    Chavez, E.R.3
  • 136
    • 37549069355 scopus 로고    scopus 로고
    • Phytate-degrading enzymes in pig nutrition
    • Selle, P.H. and Ravindran, V. (2008) Phytate-degrading enzymes in pig nutrition. Livestock Science 115, 99-122.
    • (2008) Livestock Science , vol.115 , pp. 99-122
    • Selle, P.H.1    Ravindran, V.2
  • 137
    • 0000666697 scopus 로고
    • Purification and characterization of a phytase from Bacillus subtilis (natto) N-77
    • Shimizu, M. (1992) Purification and characterization of a phytase from Bacillus subtilis (natto) N-77. Bioscience, Biotechnology and Biochemistry 56, 1266-1269.
    • (1992) Bioscience, Biotechnology and Biochemistry , vol.56 , pp. 1266-1269
    • Shimizu, M.1
  • 138
    • 0034802540 scopus 로고    scopus 로고
    • Enzyme mechanism and catalytic property of ß propeller phytase
    • Shin, S., Ha, N.-C., Oh, B.-C., Oh, T.-K. and Oh, B.-H. (2001) Enzyme mechanism and catalytic property of ß propeller phytase. Structure 9, 851-858.
    • (2001) Structure , vol.9 , pp. 851-858
    • Shin, S.1    Ha, N.-C.2    Oh, B.-C.3    Oh, T.-K.4    Oh, B.-H.5
  • 142
    • 2642525493 scopus 로고    scopus 로고
    • Effects of combining three fungal phytases with a bacterial phytase in plasma phosphorus status of weanling pigs fed a corn-soy diet
    • Stahl, C.H., Roneker, K., Pond, W.G. and Lei, X.G. (2004) Effects of combining three fungal phytases with a bacterial phytase in plasma phosphorus status of weanling pigs fed a corn-soy diet. Journal of Animal Science 82, 1725-1731.
    • (2004) Journal of Animal Science , vol.82 , pp. 1725-1731
    • Stahl, C.H.1    Roneker, K.2    Pond, W.G.3    Lei, X.G.4
  • 143
    • 0028278712 scopus 로고
    • Two distinct molecular forms of phytase from Klebsiella aerogenes: evidence for unusually small active enzyme peptide
    • Tambe, S.M., Kaklij, G.S., Keklar, S.M. and Parekh, L.J. (1994) Two distinct molecular forms of phytase from Klebsiella aerogenes: evidence for unusually small active enzyme peptide. Journal of Fermentation and Bioengineering 77, 23-27.
    • (1994) Journal of Fermentation and Bioengineering , vol.77 , pp. 23-27
    • Tambe, S.M.1    Kaklij, G.S.2    Keklar, S.M.3    Parekh, L.J.4
  • 144
    • 0033854732 scopus 로고    scopus 로고
    • Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure
    • Tomschy, A., Tessier, M., Wyss, M., Brugger, R., Broger, C., Schnoebelein, L. et al. (2000a) Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure. Protein Science 9, 1304-1311.
    • (2000) Protein Science , vol.9 , pp. 1304-1311
    • Tomschy, A.1    Tessier, M.2    Wyss, M.3    Brugger, R.4    Broger, C.5    Schnoebelein, L.6
  • 145
    • 18244425080 scopus 로고    scopus 로고
    • Active site residue 297 of Aspergillus niger phytase critically affects the catalytic properties
    • Tomschy, A., Wyss, M., Kostrewa, D., Vogel, K., Tessier, M., Höfer, S. et al. (2000b) Active site residue 297 of Aspergillus niger phytase critically affects the catalytic properties. FEBS Letters 472, 169-172.
    • (2000) FEBS Letters , vol.472 , pp. 169-172
    • Tomschy, A.1    Wyss, M.2    Kostrewa, D.3    Vogel, K.4    Tessier, M.5    Höfer, S.6
  • 147
    • 0034577375 scopus 로고    scopus 로고
    • Isolation and characterization of a novel phytase from Penicillium simplicissimum
    • Tseng, Y.H., Fang, T.J. and Tseng, S.M. (2000) Isolation and characterization of a novel phytase from Penicillium simplicissimum. Folia Microbiologia 45, 121-127.
    • (2000) Folia Microbiologia , vol.45 , pp. 121-127
    • Tseng, Y.H.1    Fang, T.J.2    Tseng, S.M.3
  • 148
    • 0036315591 scopus 로고    scopus 로고
    • Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis.
    • Tye, A.J., Siu, F.K., Leung, T.Y. and Lim, B.L. (2002) Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis. Applied Microbiology and Biotechnology 59, 190-197.
    • (2002) Applied Microbiology and Biotechnology , vol.59 , pp. 190-197
    • Tye, A.J.1    Siu, F.K.2    Leung, T.Y.3    Lim, B.L.4
  • 149
    • 0024237908 scopus 로고
    • Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization
    • Ullah, A.H.J. (1988) Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization. Preparative Biochemistry 18, 459-471.
    • (1988) Preparative Biochemistry , vol.18 , pp. 459-471
    • Ullah, A.H.J.1
  • 150
    • 0023493960 scopus 로고
    • Purification, N-terminal amino acid sequence and characterization of pH 2.5 optimum acid phosphatase (E.C.3.1.3.2) from Aspergillus ficuum
    • Ullah, A.H.J. and Cummins, B.J. (1987) Purification, N-terminal amino acid sequence and characterization of pH 2.5 optimum acid phosphatase (E.C.3.1.3.2) from Aspergillus ficuum. Preparative Biochemistry 17, 397-422.
    • (1987) Preparative Biochemistry , vol.17 , pp. 397-422
    • Ullah, A.H.J.1    Cummins, B.J.2
  • 151
    • 0023080759 scopus 로고
    • Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: purification and characterization
    • Ullah, A.H.J. and Gibson, D.M. (1987) Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: purification and characterization. Preparative Biochemistry 17, 63-91.
    • (1987) Preparative Biochemistry , vol.17 , pp. 63-91
    • Ullah, A.H.J.1    Gibson, D.M.2
  • 152
    • 0037418691 scopus 로고    scopus 로고
    • PhyA gene product of Aspergillus ficuum and Peniophora lycii produces dissimilar phytases
    • Ullah, A.H.J. and Sethumadhavan, K. (2003) PhyA gene product of Aspergillus ficuum and Peniophora lycii produces dissimilar phytases. Biochemical and Biophysical Research Communications 303, 463-468.
    • (2003) Biochemical and Biophysical Research Communications , vol.303 , pp. 463-468
    • Ullah, A.H.J.1    Sethumadhavan, K.2
  • 154
    • 0029610551 scopus 로고
    • Stereospecificity of inositol hexaphosphate dephosphorylation by Paramecium phytase
    • van der Kaay, J. and van Haastert, J.M. (1995) Stereospecificity of inositol hexaphosphate dephosphorylation by Paramecium phytase. Biochemical Journal 312, 907-910.
    • (1995) Biochemical Journal , vol.312 , pp. 907-910
    • van der Kaay, J.1    van Haastert, J.M.2
  • 155
    • 0025915380 scopus 로고
    • Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase
    • 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. Journal of Biological Chemistry 266, 2313-2319.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 2313-2319
    • van Etten, R.L.1    Davidson, R.2    Stevis, P.E.3    MacArthur, H.4    Moore, D.L.5
  • 156
    • 0036789458 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable and acid-stable phytase from Pichia anomala
    • Vohra, A. and Satyanarayana T. (2002) Purification and characterization of a thermostable and acid-stable phytase from Pichia anomala. World Journal of Microbiology and Biotechnology 18, 687-691.
    • (2002) World Journal of Microbiology and Biotechnology , vol.18 , pp. 687-691
    • Vohra, A.1    Satyanarayana, T.2
  • 157
    • 0036387214 scopus 로고    scopus 로고
    • Microbial phytase combined with amino acid supplementation reduces P and N excretion of growing and finishing pigs without loss of performance
    • Walz, O.P. and Pallauf, J. (2002) Microbial phytase combined with amino acid supplementation reduces P and N excretion of growing and finishing pigs without loss of performance. International Journal of Food Science and Technology 37, 835-848.
    • (2002) International Journal of Food Science and Technology , vol.37 , pp. 835-848
    • Walz, O.P.1    Pallauf, J.2
  • 159
    • 0031734945 scopus 로고    scopus 로고
    • Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase, and A. niger pH 2.5 acid phosphatase.
    • Wyss, M., Pasamontes, L., Friedlein, A., Rémy, R., Kohler, J., Kusznir, E. et al. (1998) Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase, and A. niger pH 2.5 acid phosphatase. Applied and Environmental Microbiology 64, 4446-4451.
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 4446-4451
    • Wyss, M.1    Pasamontes, L.2    Friedlein, A.3    Rémy, R.4    Kohler, J.5    Kusznir, E.6
  • 160
    • 0033051539 scopus 로고    scopus 로고
    • Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolase): catalytic properties
    • Wyss, M., Brugger, R., Kronenberger, A., Rémy, R., Fimbel, R., Oesterhelt, G. et al. (1999a) Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolase): catalytic properties. Applied and Environmental Microbiology 65, 367-373.
    • (1999) Applied and Environmental Microbiology , vol.65 , pp. 367-373
    • Wyss, M.1    Brugger, R.2    Kronenberger, A.3    Rémy, R.4    Fimbel, R.5    Oesterhelt, G.6
  • 161
    • 0032976125 scopus 로고    scopus 로고
    • Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolase): molecular size, glycosylation pattern, and engineering of proteolytic resistance
    • Wyss, M., Pasamontes, L., Friedlein, A., Rémy, R., Tessier, M., Kronenberger, A. et al. (1999b) Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolase): molecular size, glycosylation pattern, and engineering of proteolytic resistance. Applied and Environmental Microbiology 65, 359-366.
    • (1999) Applied and Environmental Microbiology , vol.65 , pp. 359-366
    • Wyss, M.1    Pasamontes, L.2    Friedlein, A.3    Rémy, R.4    Tessier, M.5    Kronenberger, A.6
  • 162
    • 26444553295 scopus 로고    scopus 로고
    • Transgenic expression of a novel M. trunculata phytase gene results in improved acquisition of organic phosphorus by Arabidopsis.
    • Xiao, K., Harrison, M.J. and Wang, Z. (2005) Transgenic expression of a novel M. trunculata phytase gene results in improved acquisition of organic phosphorus by Arabidopsis. Planta 222, 27-36.
    • (2005) Planta , vol.222 , pp. 27-36
    • Xiao, K.1    Harrison, M.J.2    Wang, Z.3
  • 163
    • 0036236132 scopus 로고    scopus 로고
    • Effects of fungal phytase on utilization of dietary protein and minerals, and dephosphorylation of phytic acid in the alimentary tract of channel catfish Ictalurus punctarus fed an all-plant protein diet
    • Yan, W., Reigh, R.C. and Xu, Z. (2002) Effects of fungal phytase on utilization of dietary protein and minerals, and dephosphorylation of phytic acid in the alimentary tract of channel catfish Ictalurus punctarus fed an all-plant protein diet. Journal of the World Aquaculture Society 33, 10-22.
    • (2002) Journal of the World Aquaculture Society , vol.33 , pp. 10-22
    • Yan, W.1    Reigh, R.C.2    Xu, Z.3
  • 164
    • 0032779947 scopus 로고    scopus 로고
    • Phytase activity in Selenomonas ruminantium: a preliminary characterization
    • Yanke, L.J., Selinger, B.L. and Cheng, K.J. (1999) Phytase activity in Selenomonas ruminantium: a preliminary characterization. Letters in Applied Microbiology 29, 20-25.
    • (1999) Letters in Applied Microbiology , vol.29 , pp. 20-25
    • Yanke, L.J.1    Selinger, B.L.2    Cheng, K.J.3
  • 165
    • 0006741866 scopus 로고    scopus 로고
    • Recombinant Pichia pastoris overexpressing bioactive phytase
    • Yao, B., Thang, C., Wang, J. and Fan, Y. (1998) Recombinant Pichia pastoris overexpressing bioactive phytase. Science in China 41, 330-336.
    • (1998) Science in China , vol.41 , pp. 330-336
    • Yao, B.1    Thang, C.2    Wang, J.3    Fan, Y.4
  • 166
    • 0001066696 scopus 로고    scopus 로고
    • Site of phytase activity in the gastrointestinal tract of young pigs
    • Yi, Z. and Kornegay, E.T. (1996) Site of phytase activity in the gastrointestinal tract of young pigs. Animal Feed Science and Technology 61, 361-368.
    • (1996) Animal Feed Science and Technology , vol.61 , pp. 361-368
    • Yi, Z.1    Kornegay, E.T.2
  • 167
    • 0030152708 scopus 로고    scopus 로고
    • Isolation and identification of phytase-producing bacterium, Enterobacter sp.4, and enzymatic properties of phytase enzyme.
    • Yoon, S.J., Choi, Y.J., Min, H.K., Cho, K.K., Kim, J.W., Lee, S.C. et al. (1996) Isolation and identification of phytase-producing bacterium, Enterobacter sp. 4, and enzymatic properties of phytase enzyme. Enzyme and Microbial Technology 18, 449-454.
    • (1996) Enzyme and Microbial Technology , vol.18 , pp. 449-454
    • Yoon, S.J.1    Choi, Y.J.2    Min, H.K.3    Cho, K.K.4    Kim, J.W.5    Lee, S.C.6
  • 168
    • 0031021981 scopus 로고    scopus 로고
    • Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate
    • Zhang, M., Zhou, M., van Etten, R.L. and Stauffacher, C.V. (1997) Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate. Biochemistry 36, 15-23.
    • (1997) Biochemistry , vol.36 , pp. 15-23
    • Zhang, M.1    Zhou, M.2    van Etten, R.L.3    Stauffacher, C.V.4
  • 169
    • 0035147455 scopus 로고    scopus 로고
    • A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization
    • Zhou, D., Chen, L.-M., Hernandez, L., Shears, S.B. and Galán, J.E. (2001) A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization. Molecular Microbiology 39, 248-259.
    • (2001) Molecular Microbiology , vol.39 , pp. 248-259
    • Zhou, D.1    Chen, L.-M.2    Hernandez, L.3    Shears, S.B.4    Galán, J.E.5
  • 170
    • 33645471516 scopus 로고    scopus 로고
    • Biochemical properties of a thermostable phytase from Neurospora crassa
    • Zhou, X., Shen, W., Zhuge, J. and Wang, Z. (2006) Biochemical properties of a thermostable phytase from Neurospora crassa. FEMS Microbiology Letters 258, 61-66.
    • (2006) FEMS Microbiology Letters , vol.258 , pp. 61-66
    • Zhou, X.1    Shen, W.2    Zhuge, J.3    Wang, Z.4
  • 172
    • 0037456581 scopus 로고    scopus 로고
    • Additivity of the effect of cereal and microbial phytases on apparent phosphorus absorption in growing pigs fed diets with marginal P supply
    • Zimmermann, B., Lantzsch, H.-J., Mosenthin, R., Biesalski, H.K. and Drochner, W. (2003) Additivity of the effect of cereal and microbial phytases on apparent phosphorus absorption in growing pigs fed diets with marginal P supply. Animal Feed Science and Technology 104, 143-152.
    • (2003) Animal Feed Science and Technology , vol.104 , pp. 143-152
    • Zimmermann, B.1    Lantzsch, H.-J.2    Mosenthin, R.3    Biesalski, H.K.4    Drochner, W.5
  • 173
    • 0001552796 scopus 로고
    • Complete enzymatic dephosphorylation of corn-soybean meal feed under simulated intestinal conditions of the turkey
    • Zyla, K., Ledoux, D.R. and Veum, T.L. (1995) Complete enzymatic dephosphorylation of corn-soybean meal feed under simulated intestinal conditions of the turkey. Journal of Agricultural and Food Chemistry 43, 288-294.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 288-294
    • Zyla, K.1    Ledoux, D.R.2    Veum, T.L.3
  • 174
    • 0345713142 scopus 로고    scopus 로고
    • Simultaneous application of phytase and xylanase to broiler feeds based on wheat: in vivo measurements of phosphorus and pentose release from wheat and wheat-based feeds
    • Zyla, K., Gogol, D., Koreleski, J., Swiatkiewicz, S. and Ledoux, D.R. (1999) Simultaneous application of phytase and xylanase to broiler feeds based on wheat: in vivo measurements of phosphorus and pentose release from wheat and wheat-based feeds. Journal of the Science of Food and Agriculture 79, 1832-1840.
    • (1999) Journal of the Science of Food and Agriculture , vol.79 , pp. 1832-1840
    • Zyla, K.1    Gogol, D.2    Koreleski, J.3    Swiatkiewicz, S.4    Ledoux, D.R.5


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