메뉴 건너뛰기




Volumn 74, Issue 2, 2010, Pages 196-203

Heterologous expression and functional characterization of a plant alkaline phytase in Pichia pastoris

Author keywords

Alkaline phytase; Animal feed; Heterologous protein expression; Phosphate contamination; Pichia pastoris; Pollen grains

Indexed keywords

PHYTASE; PHYTIC ACID;

EID: 77957752230     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.07.003     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 1642578253 scopus 로고    scopus 로고
    • Biochemical properties and substrate specificities of alkaline and histidine acid phytases
    • B.C. Oh, W.C. Choi, S. Park, Y.O. Kim, and T.K. Oh Biochemical properties and substrate specificities of alkaline and histidine acid phytases Appl. Microbiol. Biotechnol. 63 2004 362 372
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , pp. 362-372
    • Oh, B.C.1    Choi, W.C.2    Park, S.3    Kim, Y.O.4    Oh, T.K.5
  • 2
    • 0345257904 scopus 로고    scopus 로고
    • The term phytase comprises several different classes of enzymes
    • E.J. Mullaney, and A.H.J. Ullah The term phytase comprises several different classes of enzymes Biochem. Biophys. Res. Commun. 312 2003 179 184
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 179-184
    • Mullaney, E.J.1    Ullah, A.H.J.2
  • 3
    • 0036392241 scopus 로고    scopus 로고
    • Molecular and catalytic properties of phytate-degrading enzymes (phytases)
    • U. Konietzny, and R. Greiner Molecular and catalytic properties of phytate-degrading enzymes (phytases) Int. J. Food Sci. Technol. 37 2002 791 812
    • (2002) Int. J. Food Sci. Technol. , vol.37 , pp. 791-812
    • Konietzny, U.1    Greiner, R.2
  • 6
    • 0026535321 scopus 로고
    • Hydrolysis of phosphate monoesters: A biological problem with multiple chemical solutions
    • J.B. Vincent, M.W. Crowder, and B.A. Averill Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions Trends Biochem.Sci. 17 1992 105 110
    • (1992) Trends Biochem.Sci. , vol.17 , pp. 105-110
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 7
    • 38349148383 scopus 로고    scopus 로고
    • Inositol polyphosphates: A new frontier for regulating gene expression
    • A.R. Alcazar-Roman, and S.R. Wente Inositol polyphosphates: a new frontier for regulating gene expression Chromosoma 117 2008 1 13
    • (2008) Chromosoma , vol.117 , pp. 1-13
    • Alcazar-Roman, A.R.1    Wente, S.R.2
  • 8
    • 38549132277 scopus 로고    scopus 로고
    • Inositol derivatives: Evolution and functions
    • R.H. Michell Inositol derivatives: evolution and functions Nat. Rev. Mol. Cell Biol. 9 2008 151 161
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 151-161
    • Michell, R.H.1
  • 9
    • 40549126257 scopus 로고    scopus 로고
    • Beyond IP3 - Roles for higher order inositol phosphates in immune cell signaling
    • A.T. Miller, P.P. Chamberlain, and M.P. Cooke Beyond IP3 - roles for higher order inositol phosphates in immune cell signaling Cell Cycle 7 2008 463 467
    • (2008) Cell Cycle , vol.7 , pp. 463-467
    • Miller, A.T.1    Chamberlain, P.P.2    Cooke, M.P.3
  • 10
    • 0034645799 scopus 로고    scopus 로고
    • Myo-inositol metabolism in plants
    • F.A. Loewus, and P.P.N. Murthy Myo-inositol metabolism in plants Plant Sci. 150 2000 1 19
    • (2000) Plant Sci. , vol.150 , pp. 1-19
    • Loewus, F.A.1    Murthy, P.P.N.2
  • 11
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signaling
    • M.J. Berridge Inositol trisphosphate and calcium signaling Nature 361 1993 315 325
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 13
    • 0001251469 scopus 로고
    • Localization of constitutive phytases in lily pollen and properties of the pH 8 form
    • B.G. Baldi, J.J. Scott, J.D. Everard, and F.A. Loewus Localization of constitutive phytases in lily pollen and properties of the pH 8 form Plant Sci. 56 1988 137 147
    • (1988) Plant Sci. , vol.56 , pp. 137-147
    • Baldi, B.G.1    Scott, J.J.2    Everard, J.D.3    Loewus, F.A.4
  • 14
    • 33747879395 scopus 로고    scopus 로고
    • Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase (MINPP)
    • B.D. Mehta, S.P. Jog, S.C. Johnson, and P.P.N. Murthy Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase (MINPP) Phytochemistry 67 2006 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
  • 15
    • 0034767777 scopus 로고    scopus 로고
    • Biotechnological development of effective phytases for mineral nutrition and environmental protection
    • X.G. Lei, and C.H. Stahl Biotechnological development of effective phytases for mineral nutrition and environmental protection Appl. Microbiol. Biotechnol. 57 2001 474 481
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 474-481
    • Lei, X.G.1    Stahl, C.H.2
  • 17
    • 0015140454 scopus 로고
    • Effect of supplemental phytase on the utilization of phytate phosphorus by chicks
    • T.S. Nelson, T.R. Shieh, R.J. Wodzinski, and J.H. Ware Effect of supplemental phytase on the utilization of phytate phosphorus by chicks J. Nutr. 101 1971 1289 1293
    • (1971) J. Nutr. , vol.101 , pp. 1289-1293
    • Nelson, T.S.1    Shieh, T.R.2    Wodzinski, R.J.3    Ware, J.H.4
  • 18
    • 23744459359 scopus 로고    scopus 로고
    • Alkaline phytase from lily pollen: Investigation of biochemical properties
    • S.P. Jog, B.G. Garchow, B.D. Mehta, and P.P.N. Murthy Alkaline phytase from lily pollen: investigation of biochemical properties Arch. Biochem. Biophys. 440 2005 133 140
    • (2005) Arch. Biochem. Biophys. , vol.440 , pp. 133-140
    • Jog, S.P.1    Garchow, B.G.2    Mehta, B.D.3    Murthy, P.P.N.4
  • 19
    • 0032789940 scopus 로고    scopus 로고
    • A new protein folding screen: Application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase
    • N. Armstrong, A. De Lencastre, and E. Gouaux A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase Protein Sci. 8 1999 1475 1483
    • (1999) Protein Sci. , vol.8 , pp. 1475-1483
    • Armstrong, N.1    De Lencastre, A.2    Gouaux, E.3
  • 22
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • J.L. Cereghino, and J.M. Cregg Heterologous protein expression in the methylotrophic yeast Pichia pastoris FEMS Microbiol. Rev. 24 2000 45 66
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 23
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: A useful experimental tool in protein engineering and production
    • R. Daly, and M.T.W. Hearn Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production J. Mol. Recognit. 18 2005 119 138
    • (2005) J. Mol. Recognit. , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.W.2
  • 24
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • S. Macauley-Patrick, M.L. Fazenda, B. McNeil, and L.M. Harvey Heterologous protein production using the Pichia pastoris expression system Yeast 22 2005 249 270
    • (2005) Yeast , vol.22 , pp. 249-270
    • MacAuley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 27
    • 0028675620 scopus 로고
    • Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen
    • L. Barrientos, J.J. Scott, and P.P.N. Murthy Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen Plant Physiol. 106 1994 1489 1495
    • (1994) Plant Physiol. , vol.106 , pp. 1489-1495
    • Barrientos, L.1    Scott, J.J.2    Murthy, P.P.N.3
  • 28
    • 0023663451 scopus 로고
    • Compilation and comparison of the sequence context around the AUG startcodons in Saccharomyces cerevisiae mRNAs
    • R. Hamilton, C.K. Watanabe, and H.A. de Boer Compilation and comparison of the sequence context around the AUG startcodons in Saccharomyces cerevisiae mRNAs Nucleic Acids Res. 15 1987 3581 3593
    • (1987) Nucleic Acids Res. , vol.15 , pp. 3581-3593
    • Hamilton, R.1    Watanabe, C.K.2    De Boer, H.A.3
  • 29
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • USA
    • A. Varshavsky The N-end rule: functions, mysteries, uses Proc. Natl. Acad. Sci. USA 93 1996 12142 12149
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 30
    • 33947713897 scopus 로고    scopus 로고
    • The N-end rule pathway for regulated proteolysis: Prokaryotic and eukaryotic strategies
    • A. Mogk, R. Schmidt, and B. Bukau The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies Trends Cell Biol. 17 2007 165 172
    • (2007) Trends Cell Biol. , vol.17 , pp. 165-172
    • Mogk, A.1    Schmidt, R.2    Bukau, B.3
  • 32
    • 0032580437 scopus 로고    scopus 로고
    • An improved protocol for the preparation of yeast cells for transformation by electroporation
    • J.R. Thompson, E. Register, J. Curotto, M. Kurtz, and R. Kelly An improved protocol for the preparation of yeast cells for transformation by electroporation Yeast 14 1998 565 571
    • (1998) Yeast , vol.14 , pp. 565-571
    • Thompson, J.R.1    Register, E.2    Curotto, J.3    Kurtz, M.4    Kelly, R.5
  • 33
    • 0347915684 scopus 로고    scopus 로고
    • High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol
    • S. Wu, and G. Letchworth High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol BioTechniques 36 2004 152 154
    • (2004) BioTechniques , vol.36 , pp. 152-154
    • Wu, S.1    Letchworth, G.2
  • 34
    • 0031615384 scopus 로고    scopus 로고
    • Transformation
    • J.M. Cregg, and K.A. Russell Transformation D.R. Higgins, J.M. Cregg, Pichia Protocols 1998 Humana Press Totowa 27 39
    • (1998) Pichia Protocols , pp. 27-39
    • Cregg, J.M.1    Russell, K.A.2
  • 35
    • 0023002780 scopus 로고
    • Factors enhancing genetic-transformation of intact yeast-cells modify cell-wall porosity
    • B. Brzobohaty, and L. Kovac Factors enhancing genetic-transformation of intact yeast-cells modify cell-wall porosity J. Gen. Microbiol. 132 1986 3089 3093
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 3089-3093
    • Brzobohaty, B.1    Kovac, L.2
  • 36
    • 0004353266 scopus 로고
    • Transformation of intact yeast-cells treated with alkali cations or thiol compounds
    • H. Ito, K. Murata, and A. Kimura Transformation of intact yeast-cells treated with alkali cations or thiol compounds Agric. Biol. Chem. 48 1984 341 347
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 341-347
    • Ito, H.1    Murata, K.2    Kimura, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.