메뉴 건너뛰기




Volumn 77, Issue 20, 2011, Pages 7316-7320

Improvement in the thermostability of D-psicose 3-epimerase from Agrobacterium tumefaciens by random and site-directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

AGROBACTERIUM TUMEFACIENS; AROMATIC STACKING INTERACTIONS; CONVERSION YIELD; OPERATION TIME; PSICOSE; SITE DIRECTED MUTAGENESIS; WILD-TYPE ENZYMES;

EID: 82955240007     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.05566-11     Document Type: Article
Times cited : (62)

References (27)
  • 1
    • 0001682349 scopus 로고
    • The fate of cane juice simple sugars during molasses formation IV. Probable conversion of D-fructose to D-psicose
    • Binkley, W. W. 1963. The fate of cane juice simple sugars during molasses formation. IV. Probable conversion of D-fructose to D-psicose. Int. Sugar J. 65:105-106.
    • (1963) Int. Sugar J. , vol.65 , pp. 105-106
    • Binkley, W.W.1
  • 2
    • 28944434107 scopus 로고    scopus 로고
    • Boric acid as a mobile phase additive for high performance liquid chromatography separation of ribose, arabinose and ribulose
    • De Muynck, C., J. Beauprez, W. Soetaert, and E. J. Vandamme. 2006. Boric acid as a mobile phase additive for high performance liquid chromatography separation of ribose, arabinose and ribulose. J. Chromatogr. A 1101:115- 121.
    • (2006) J. Chromatogr. A , vol.1101 , pp. 115-121
    • De Muynck, C.1    Beauprez, J.2    Soetaert, W.3    Vandamme, E.J.4
  • 4
    • 11144350760 scopus 로고
    • The occurrence of D-ribohexulose in Itea ilicifolia, Itea virginica, and Itea yunnanensis
    • Hough, L., and B. E. Stacey. 1963. The occurrence of D-ribohexulose in Itea ilicifolia, Itea virginica, and Itea yunnanensis. Phytochemistry 2:315-320.
    • (1963) Phytochemistry , vol.2 , pp. 315-320
    • Hough, L.1    Stacey, B.E.2
  • 6
    • 0028984722 scopus 로고
    • Preparation of D-psicose from D-fructose by immobilized D-tagatose 3-epimerase
    • Itoh, H., T. Sato, and K. Izumori. 1995. Preparation of D-psicose from D-fructose by immobilized D-tagatose 3-epimerase. J. Ferment. Bioeng. 80:101-103.
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 101-103
    • Itoh, H.1    Sato, T.2    Izumori, K.3
  • 7
    • 77953869815 scopus 로고    scopus 로고
    • Enhancement of the thermostability of a recombinant beta-agarase, AgaB, from Zobellia galactanivorans by random mutagenesis
    • Jang, M. K., et al. 2010. Enhancement of the thermostability of a recombinant beta-agarase, AgaB, from Zobellia galactanivorans by random mutagenesis. Biotechnol. Lett. 32:943-949.
    • (2010) Biotechnol. Lett. , vol.32 , pp. 943-949
    • Jang, M.K.1
  • 8
    • 27644547321 scopus 로고    scopus 로고
    • Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis Biosci
    • Khan, M. I., et al. 2005. Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis. Biosci. Biotechnol. Biochem. 69:1861-1870.
    • (2005) Biotechnol. Biochem. , vol.69 , pp. 1861-1870
    • Khan, M.I.1
  • 9
    • 33144484509 scopus 로고    scopus 로고
    • Characterization of an Agrobacterium tumefaciens D-psicose 3-epimerase that converts D-fructose to D-psicose
    • Kim, H. J., E. K. Hyun, Y. S. Kim, Y. J. Lee, and D. K. Oh. 2006. Characterization of an Agrobacterium tumefaciens D-psicose 3-epimerase that converts D-fructose to D-psicose. Appl. Environ. Microbiol. 72:981-985.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 981-985
    • Kim, H.J.1    Hyun, E.K.2    Kim, Y.S.3    Lee, Y.J.4    Oh, D.K.5
  • 10
    • 33746929133 scopus 로고    scopus 로고
    • Crystal structure of D-psicose 3-epimerase from Agrobacterium tumefaciens and its complex with true substrate D-fructose: a pivotal role of metal in catalysis, an active site for the non-phosphorylated substrate, and its conformational changes
    • Kim, K., H. J. Kim, D. K. Oh, S. S. Cha, and S. Rhee. 2006. Crystal structure of D-psicose 3-epimerase from Agrobacterium tumefaciens and its complex with true substrate D-fructose: a pivotal role of metal in catalysis, an active site for the non-phosphorylated substrate, and its conformational changes. J. Mol. Biol. 361:920-931.
    • (2006) J. Mol. Biol. , vol.361 , pp. 920-931
    • Kim, K.1    Kim, H.J.2    Oh, D.K.3    Cha, S.S.4    Rhee, S.5
  • 11
    • 42149088826 scopus 로고    scopus 로고
    • Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR
    • Kim, M. S., and X. G. Lei. 2008. Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR. Appl. Microbiol. Biotechnol. 79: 69-75.
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , pp. 69-75
    • Kim, M.S.1    Lei, X.G.2
  • 12
    • 44249103017 scopus 로고    scopus 로고
    • Conversion shift of D-fructose to D-psicose for enzyme-catalyzed epimerization by addition of borate
    • Kim, N. H., et al. 2008. Conversion shift of D-fructose to D-psicose for enzyme-catalyzed epimerization by addition of borate. Appl. Environ. Microbiol. 74:3008-3013.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 3008-3013
    • Kim, N.H.1
  • 13
    • 0042530128 scopus 로고    scopus 로고
    • Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance
    • Kim, Y. W., et al. 2003. Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance. Appl. Environ. Microbiol. 69:4866- 4874.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4866-4874
    • Kim, Y.W.1
  • 14
    • 34547920744 scopus 로고    scopus 로고
    • High production of D-tagatose by the addition of boric acid
    • Lim, B. C., H. J. Kim, and D. K. Oh. 2007. High production of D-tagatose by the addition of boric acid. Biotechnol. Prog. 23:824-828.
    • (2007) Biotechnol. Prog. , vol.23 , pp. 824-828
    • Lim, B.C.1    Kim, H.J.2    Oh, D.K.3
  • 15
    • 67349177033 scopus 로고    scopus 로고
    • A stable immobilized D-psicose 3-epimerase for the production of D-psicose in the presence of borate
    • Lim, B. C., H. J. Kim, and D. K. Oh. 2009. A stable immobilized D-psicose 3-epimerase for the production of D-psicose in the presence of borate. Process Biochem. 44:822-828.
    • (2009) Process Biochem , vol.44 , pp. 822-828
    • Lim, B.C.1    Kim, H.J.2    Oh, D.K.3
  • 16
    • 0000224283 scopus 로고    scopus 로고
    • CHARMM: the energy function and its parameterization with an overview of the program
    • P. von Rague Schleyer et al. (ed.) John Wiley & Sons, Chichester United Kingdom
    • MacKerell, A. D., Jr., et al. 1998. CHARMM: the energy function and its parameterization with an overview of the program, p. 271-277. In P. von Rague Schleyer et al. (ed.), The encyclopedia of computational chemistry, vol. 1. John Wiley & Sons, Chichester, United Kingdom.
    • (1998) The encyclopedia of computational chemistry , vol.1 , pp. 271-277
    • MacKerell Jr., A.D.1
  • 17
    • 0035536718 scopus 로고    scopus 로고
    • Dietary D-psicose, a C-3 epimer of D-fructose, suppresses the activity of hepatic lipogenic enzymes in rats
    • Matsuo, T., et al. 2001. Dietary D-psicose, a C-3 epimer of D-fructose, suppresses the activity of hepatic lipogenic enzymes in rats. Asia Pac. Clin. Nutr. 10:233-237.
    • (2001) Asia Pac. Clin. Nutr. , vol.10 , pp. 233-237
    • Matsuo, T.1
  • 19
    • 0032546782 scopus 로고    scopus 로고
    • π-stacking interactions Alive and well in proteins
    • McGaughey, G. B., M. Gagne, and A. K. Rappe. 1998 π-stacking interactions. Alive and well in proteins. J. Biol. Chem. 273:15458-15463.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3
  • 20
    • 84982338569 scopus 로고
    • Chromatographic analyses of the free amino acids, organic acids and sugars in wheat plant extracts
    • Miller, B. S., and T. Swain. 1960. Chromatographic analyses of the free amino acids, organic acids and sugars in wheat plant extracts. J. Sci. Food Agric. 11:344-348.
    • (1960) J. Sci. Food Agric. , vol.11 , pp. 344-348
    • Miller, B.S.1    Swain, T.2
  • 21
    • 78650837146 scopus 로고    scopus 로고
    • Three amino acid changes contribute markedly to the thermostability of beta-glucosidase BglC from Thermobifida fusca
    • Pei, X. Q., Z. L. Yi, C. G. Tang, and Z. L. Wu. 2011. Three amino acid changes contribute markedly to the thermostability of beta-glucosidase BglC from Thermobifida fusca. Bioresour. Technol. 102:3337-3342.
    • (2011) Bioresour. Technol. , vol.102 , pp. 3337-3342
    • Pei, X.Q.1    Yi, Z.L.2    Tang, C.G.3    Wu, Z.L.4
  • 22
    • 47349126199 scopus 로고    scopus 로고
    • Influence of a rare sugar, D-psicose, on the physicochemical and functional properties of an aerated food system containing egg albumen
    • Sun, Y., S. Hayakawa, M. Ogawa, K. Fukada, and K. Izumori. 2008. Influence of a rare sugar, D-psicose, on the physicochemical and functional properties of an aerated food system containing egg albumen. J. Agric. Food Chem. 56:4789-4796.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 4789-4796
    • Sun, Y.1    Hayakawa, S.2    Ogawa, M.3    Fukada, K.4    Izumori, K.5
  • 23
    • 0034302040 scopus 로고    scopus 로고
    • Mass production of D-psicose from D-fructose by a continuous bioreactor system using immobilized D-tagatose 3-epimerase
    • Takeshita, K., A. Suga, G. Takada, and K. Izumori. 2000. Mass production of D-psicose from D-fructose by a continuous bioreactor system using immobilized D-tagatose 3-epimerase. J. Biosci. Bioeng. 90:453-455.
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 453-455
    • Takeshita, K.1    Suga, A.2    Takada, G.3    Izumori, K.4
  • 24
    • 61349159248 scopus 로고    scopus 로고
    • An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds
    • Vieira, D. S., and L. Degre've. 2009. An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds. Mol. Phys. 107:59-69.
    • (2009) Mol. Phys. , vol.107 , pp. 59-69
    • Vieira, D.S.1    Degre've, L.2
  • 25
    • 67349146995 scopus 로고    scopus 로고
    • Characterization of D-tagatose-3-epimerase from Rhodobacter sphaeroides that converts D-fructose into D-psicose
    • Zhang, L., W. Mu, B. Jiang, and T. Zhang. 2009. Characterization of D-tagatose-3-epimerase from Rhodobacter sphaeroides that converts D-fructose into D-psicose. Biotechnol. Lett. 31:857-862.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 857-862
    • Zhang, L.1    Mu, W.2    Jiang, B.3    Zhang, T.4
  • 26
    • 77955528014 scopus 로고    scopus 로고
    • L-Ribulose production by an Escherichia coli harboring L-arabinose isomerase from Bacillus licheniformis
    • Zhang, Y. W., M. Jeya, and J. K. Lee. 2010. L-Ribulose production by an Escherichia coli harboring L-arabinose isomerase from Bacillus licheniformis. Appl. Microbiol. Biotechnol. 87:1993-1999.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1993-1999
    • Zhang, Y.W.1    Jeya, M.2    Lee, J.K.3
  • 27
    • 77955657417 scopus 로고    scopus 로고
    • Improving the thermostability of Geobacillus stearothermophilus xylanase XT6 by directed evolution and site-directed mutagenesis
    • Zhang, Z. G., Z. L. Yi, X. Q. Pei, and Z. L. Wu. 2010. Improving the thermostability of Geobacillus stearothermophilus xylanase XT6 by directed evolution and site-directed mutagenesis. Bioresour. Technol. 101:9272-9278.
    • (2010) Bioresour. Technol. , vol.101 , pp. 9272-9278
    • Zhang, Z.G.1    Yi, Z.L.2    Pei, X.Q.3    Wu, Z.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.