메뉴 건너뛰기




Volumn 76, Issue 19, 2010, Pages 6423-6430

Design of thermostable beta-propeller phytases with activity over a broad range of pHs and their overproduction by pichia pastoris

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ANIMAL DIET; BACILLUS SUBTILIS; FEED ADDITIVES; GENBANK; GLYCOSYLATED; PELLETING PROCESS; PH RANGE; PHYTASES; PICHIA PASTORIS; PRE-TREATMENT; RESIDUAL ACTIVITY; SURFACE LOOPS; TOTAL CHARGE;

EID: 78049285754     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00253-10     Document Type: Article
Times cited : (47)

References (40)
  • 1
    • 67549134221 scopus 로고    scopus 로고
    • Comparative thermostability of mesophilic and thermophilic alcohol dehydrogenases: Stability-determining roles of proline residues and loop conformations
    • Barzegar, A., A. A. Moosavi-Movahedi, J. Z. Pedersen, and M. Miroliaei. 2009. Comparative thermostability of mesophilic and thermophilic alcohol dehydrogenases: stability-determining roles of proline residues and loop conformations. Enzyme Microb. Technol. 45:73-79.
    • (2009) Enzyme Microb. Technol. , vol.45 , pp. 73-79
    • Barzegar, A.1    Moosavi-Movahedi, A.A.2    Pedersen, J.Z.3    Miroliaei, M.4
  • 3
    • 33745698181 scopus 로고    scopus 로고
    • Generation and analysis of proline mutants in protein G
    • Choi, E. J., and S. L. Mayo. 2006. Generation and analysis of proline mutants in protein G. Protein Eng. Des. Sel. 19:285-289.
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 285-289
    • Choi, E.J.1    Mayo, S.L.2
  • 4
    • 2942674460 scopus 로고    scopus 로고
    • Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley aα-glucosidase
    • Clark, S. E., E. H. Muslin, and C. H. Henson. 2004. Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley aα-glucosidase. Protein Eng. Des. Sel. 17:245-249.
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 245-249
    • Clark, S.E.1    Muslin, E.H.2    Henson, C.H.3
  • 5
    • 3242879177 scopus 로고    scopus 로고
    • Imoltalk: An interactive, Internetbased protein structure analysis server
    • Diemand, A. V., and H. Scheib. 2004. iMolTalk: an interactive, Internetbased protein structure analysis server. Nucleic Acids Res. 32:W512-W516.
    • (2004) Nucleic Acids Res. , vol.32
    • Diemand, A.V.1    Scheib, H.2
  • 7
    • 56749131249 scopus 로고    scopus 로고
    • Gene cloning and characterization of a thermostable phytase from Bacillus subtilis US417 and assessment of its potential as a feed additive in comparison with a commercial enzyme
    • Farhat, A., H. Chouayekh, M. B. Farhat, K. Bouchaala, and S. Bejar. 2008. Gene cloning and characterization of a thermostable phytase from Bacillus subtilis US417 and assessment of its potential as a feed additive in comparison with a commercial enzyme. Mol. Biotechnol. 40:127-135.
    • (2008) Mol. Biotechnol. , vol.40 , pp. 127-135
    • Farhat, A.1    Chouayekh, H.2    Farhat, M.B.3    Bouchaala, K.4    Bejar, S.5
  • 8
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C. H., and Y. Subarrow. 1925. The colorimetric determination of phosphorus. J. Biol. Chem. 66:375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subarrow, Y.2
  • 9
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R., and W. Braun. 1998. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 19:319-333.
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 14
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb- Viewer: An environment for comparative protein modeling
    • Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-Pdb- Viewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 15
    • 39149116352 scopus 로고    scopus 로고
    • Effect of glycosylation on biochemical characterization of recombinant phytase expressed in Pichia pastoris
    • Guo, M., H. Hang, T. Zhu, Y. Zhuang, J. Chu, and S. Zhang. 2008. Effect of glycosylation on biochemical characterization of recombinant phytase expressed in Pichia pastoris. Enzyme Microb. Technol. 42:340-345.
    • (2008) Enzyme Microb. Technol. , vol.42 , pp. 340-345
    • Guo, M.1    Hang, H.2    Zhu, T.3    Zhuang, Y.4    Chu, J.5    Zhang, S.6
  • 16
    • 0033950597 scopus 로고    scopus 로고
    • Crystal structures of a novel thermostable phytase in partially and fully calcium-loaded states
    • Ha, N. C., B. C. Oh, S. Shin, H. J. Kim, T. K. Oh, Y. O. Kim, K. Y. Choi, and B. H. Oh. 2000. Crystal structures of a novel thermostable phytase in partially and fully calcium-loaded states. Nat. Struct. Biol. 7:147-153.
    • (2000) Nat. Struct. Biol. , 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    Choi, K.Y.7    Oh, B.H.8
  • 17
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall, T. A. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41:95-98.
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 18
    • 0344289519 scopus 로고    scopus 로고
    • Role of glycosylation in the functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris
    • Han, Y. M., and X. G. Lei. 1999. Role of glycosylation in the functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris. Arch. Biochem. Biophys. 364:83-90.
    • (1999) Arch. Biochem. Biophys. , vol.364 , pp. 83-90
    • Han, Y.M.1    Lei, X.G.2
  • 19
    • 0019287872 scopus 로고
    • Thermostability and aliphatic index of globular proteins
    • Ikai, A. 1980. Thermostability and aliphatic index of globular proteins. J. Biochem. 88:1895-1898.
    • (1980) J. Biochem. , vol.88 , pp. 1895-1898
    • Ikai, A.1
  • 22
    • 0031747416 scopus 로고    scopus 로고
    • Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis
    • Kerovuo, J., M. Lauraeus, P. Nurminen, N. Kalkkinen, and J. Apajalahti. 1998. Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis. Appl. Environ. Microbiol. 64:2079-2085.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2079-2085
    • Kerovuo, J.1    Lauraeus, M.2    Nurminen, P.3    Kalkkinen, N.4    Apajalahti, J.5
  • 23
    • 0031982859 scopus 로고    scopus 로고
    • Purification and properties of a thermostable phytase from Bacillus sp. DS11
    • Kim, Y. O., H. K. Kim, K. S. Bae, J. H. Yu, and T. K. Oh. 1998. Purification and properties of a thermostable phytase from Bacillus sp. DS11. Enzyme Microb. Technol. 22:2-7.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 2-7
    • Kim, Y.O.1    Kim, H.K.2    Bae, K.S.3    Yu, J.H.4    Oh, T.K.5
  • 24
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S., C.-J. Tsai, and R. Nussinov. 2000. Factors enhancing protein thermostability. Protein Eng. 13:179-191.
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.-J.2    Nussinov, R.3
  • 26
    • 0033963277 scopus 로고    scopus 로고
    • From DNA sequence to improved functionality: Using protein sequence comparisons to rapidly design a thermostable consensus phytase
    • Lehmann, M., D. Kostrewa, M. Wyss, R. Brugger, A. D'Arcy, L. Pasamontes, and A. P. van Loon. 2000. From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. Protein Eng. 13:49-57.
    • (2000) Protein Eng. , vol.13 , pp. 49-57
    • Lehmann, M.1    Kostrewa, D.2    Wyss, M.3    Brugger, R.4    D'Arcy, A.5    Pasamontes, L.6    Van Loon, A.P.7
  • 27
    • 0034767777 scopus 로고    scopus 로고
    • Biotechnological development of effective phytases for mineral nutrition and environmental protection
    • Lei, X. G., and C. H. Stahl. 2001. Biotechnological development of effective phytases for mineral nutrition and environmental protection. Appl. Microbiol. Biotechnol. 57:474-481.
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 474-481
    • Lei, X.G.1    Stahl, C.H.2
  • 29
    • 33645109741 scopus 로고    scopus 로고
    • Observation of a unique pattern of bifurcated hydrogen bonds in the crystal structures of the N-glycoprotein linkage region models
    • Loganathan, D., and U. Aich. 2006. Observation of a unique pattern of bifurcated hydrogen bonds in the crystal structures of the N-glycoprotein linkage region models. Glycobiology 16:343-348.
    • (2006) Glycobiology , vol.16 , pp. 343-348
    • Loganathan, D.1    Aich, U.2
  • 30
    • 84890669450 scopus 로고    scopus 로고
    • Phytases: Attributes, catalytic mechanisms and applications
    • L. Turner, A. E. Richardson, and E. J. Mullaney (ed.), CAB International, Oxfordshire, United Kingdom
    • Mullaney, E. J., and A. H. Ullah. 2007. Phytases: attributes, catalytic mechanisms and applications, p. 97-110. In L. Turner, A. E. Richardson, and E. J. Mullaney (ed.), Inositol phosphates: linking agriculture and the environment. CAB International, Oxfordshire, United Kingdom.
    • (2007) Inositol Phosphates: Linking Agriculture and the Environment , pp. 97-110
    • Mullaney, E.J.1    Ullah, A.H.2
  • 31
    • 0028196642 scopus 로고
    • Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2
    • Ortmann, D., M. Ohuchi, H. Angliker, E. Shaw, W. Garten, and H. D. Klenk. 1994. Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2. J. Virol. 68:2772-2776.
    • (1994) J. Virol. , vol.68 , pp. 2772-2776
    • Ortmann, D.1    Ohuchi, M.2    Angliker, H.3    Shaw, E.4    Garten, W.5    Klenk, H.D.6
  • 34
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., J. Kopp, N. Guex, and M. C. Peitsch. 2003. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31:3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 35
    • 0034802540 scopus 로고    scopus 로고
    • Enzyme mechanism and catalytic property of beta propeller phytase
    • Shin, S., N. C. Ha, B. C. Oh, T. K. Oh, and B. H. Oh. 2001. Enzyme mechanism and catalytic property of beta 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
  • 36
    • 0002184856 scopus 로고
    • Strategies for optimizing protein expression and secretion in the methylotrophic yeast Pichia pastoris
    • R. H. Baltz, G. D. Hegeman, and P. L. Skatrud (ed.), American Society for Microbiology, Washington, DC
    • Sreekrishna, K. 1993. Strategies for optimizing protein expression and secretion in the methylotrophic yeast Pichia pastoris, p. 119-126. In R. H. Baltz, G. D. Hegeman, and P. L. Skatrud (ed.), Industrial microorganisms: basic and applied molecular genetics. American Society for Microbiology, Washington, DC.
    • (1993) Industrial Microorganisms: Basic and Applied Molecular Genetics , pp. 119-126
    • Sreekrishna, K.1
  • 37
    • 38849157945 scopus 로고    scopus 로고
    • Development of a thermostable glucose dehydrogenase by a structureguided consensus concept
    • Vázquez-Figueroa, E., J. Chaparro-Riggers, and A. S. Bommarius. 2007. Development of a thermostable glucose dehydrogenase by a structureguided consensus concept. Chembiochem 8:2295-2301.
    • (2007) Chembiochem , vol.8 , pp. 2295-2301
    • Vázquez-Figueroa, E.1    Chaparro-Riggers, J.2    Bommarius, A.S.3
  • 38
    • 0027980359 scopus 로고
    • Molecular basis of cooperativity in protein folding. V. Thermodynamic and structural conditions for the stabilization of compact denatured states
    • Xie, D., and E. Freire. 1994. Molecular basis of cooperativity in protein folding. V. Thermodynamic and structural conditions for the stabilization of compact denatured states. Proteins 19:291-301.
    • (1994) Proteins , vol.19 , pp. 291-301
    • Xie, D.1    Freire, E.2
  • 39
    • 13244268400 scopus 로고    scopus 로고
    • High level expression of a recombinant acid phytase gene in Pichia pastoris
    • Xiong, A. S., Q. H. Yao, R. H. Peng, P. L. Han, Z. M. Cheng, and Y. Li. 2005. High level expression of a recombinant acid phytase gene in Pichia pastoris. J. Appl. Microbiol. 98:418-428.
    • (2005) J. Appl. Microbiol. , vol.98 , pp. 418-428
    • Xiong, A.S.1    Yao, Q.H.2    Peng, R.H.3    Han, P.L.4    Cheng, Z.M.5    Li, Y.6
  • 40
    • 0034182261 scopus 로고    scopus 로고
    • Synonymous codon usage in Pichia pastoris\
    • Zhao, X., K. K. Huo, and Y. Y. Li. 2000. Synonymous codon usage in Pichia pastoris. Chin. J. Biotechnol. 16:308-311.
    • (2000) Chin. J. Biotechnol. , vol.16 , pp. 308-311
    • Zhao, X.1    Huo, K.K.2    Li, Y.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.