메뉴 건너뛰기




Volumn 8, Issue 4, 2013, Pages 346-356

Thermostable mutant variants of Bacillus sp. 406 α-amylase generated by site-directed mutagenesis

Author keywords

amylase; Bacillus; Protein engineering; Site directed mutagenesis; Thermal stability

Indexed keywords

BACILLUS LICHENIFORMIS; BACILLUS SP.;

EID: 84873708297     PISSN: 1895104X     EISSN: 16443632     Source Type: Journal    
DOI: 10.2478/s11535-013-0142-0     Document Type: Article
Times cited : (12)

References (22)
  • 3
    • 0024795242 scopus 로고
    • Amino acid residues stabilizing a Bacillus α-amylase against irreversible thermoinactivation
    • Suzuki Y., Ito N., Yuuki T., Yamagata H., Udaka S., Amino acid residues stabilizing a Bacillus α-amylase against irreversible thermoinactivation, J. Biol. Chem., 1989, 264, 18933-18938.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18933-18938
    • Suzuki, Y.1    Ito, N.2    Yuuki, T.3    Yamagata, H.4    Udaka, S.5
  • 4
    • 33747804863 scopus 로고    scopus 로고
    • Improvement of thermostability of a calcium-free α-amylase from an alkaliphilic Bacillus sp. by protein engeneering
    • Hagihara H., Igarashi K., Hayashi Y., Kitayama K., Endo K., Ozawa T., et al., Improvement of thermostability of a calcium-free α-amylase from an alkaliphilic Bacillus sp. by protein engeneering, J. Appl. Glycosci., 2002, 49, 281-289.
    • (2002) J. Appl. Glycosci. , vol.49 , pp. 281-289
    • Hagihara, H.1    Igarashi, K.2    Hayashi, Y.3    Kitayama, K.4    Endo, K.5    Ozawa, T.6
  • 5
    • 32944455102 scopus 로고    scopus 로고
    • Thermostability enhancement and change in starch hydrolysis profile of the maltohexaoseforming amylase of Bacillus stearothermophilus US100 strain
    • Ben Ali M., Khemakhem B., Robert X., Haser R., Bejar S., Thermostability enhancement and change in starch hydrolysis profile of the maltohexaoseforming amylase of Bacillus stearothermophilus US100 strain, Biochem. J., 2006, 394, 51-56.
    • (2006) Biochem. J. , vol.394 , pp. 51-56
    • Ben Ali, M.1    Khemakhem, B.2    Robert, X.3    Haser, R.4    Bejar, S.5
  • 6
    • 0037393130 scopus 로고    scopus 로고
    • Improving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis
    • Shiau R. J., Hung H. C., Jeang C. L., Improving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis, Appl. Environ. Microbiol., 2003, 69, 383-385.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 383-385
    • Shiau, R.J.1    Hung, H.C.2    Jeang, C.L.3
  • 8
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J. D., Gibson T. J., Plewniak F., Jeanmougin F., Higgins D. G., The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools, Nucleic Acids Res., 1997, 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 9
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D. I., Métoz F., ESPript: analysis of multiple sequence alignments in PostScript, Bioinformatics, 1999, 15, 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4
  • 10
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: a web-based environment for protein structure homology modeling
    • Arnold K., Bordoli L., Kopp J., Schwede T., The SWISS-MODEL Workspace: a web-based environment for protein structure homology modeling, Bioinformatics, 2006, 22, 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 11
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu H. C., Heppel L. A., The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts, J. Biol. Chem., 1965, 240, 3685-3692.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 12
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G. L., Use of dinitrosalicylic acid reagent for determination of reducing sugar, Anal. Chem, 1959, 31, 426-429.
    • (1959) Anal. Chem , vol.31 , pp. 426-429
    • Miller, G.L.1
  • 14
    • 33746870417 scopus 로고    scopus 로고
    • Comparison of the wild-type α-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of Bacillus α-amylase
    • Lee S., Oneda H., Minoda M., Tanaka A., Inouye K. J., Comparison of the wild-type α-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of Bacillus α-amylase, Biochem., 2006, 139, 997-1005.
    • (2006) Biochem. , vol.139 , pp. 997-1005
    • Lee, S.1    Oneda, H.2    Minoda, M.3    Tanaka, A.4    Inouye, K.J.5
  • 15
    • 77956593720 scopus 로고    scopus 로고
    • A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability
    • Siddiqui K. S., Poljak A., De Francisci D., Guerriero G., Pilak O., Burg D., et al., A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability, Protein Eng. Des. Sel., 2010, 23, 769-780.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 769-780
    • Siddiqui, K.S.1    Poljak, A.2    de Francisci, D.3    Guerriero, G.4    Pilak, O.5    Burg, D.6
  • 17
    • 0030986231 scopus 로고    scopus 로고
    • Hyperthermostable mutants of Bacillus licheniformis α-amylase: thermodynamic studies and structural interpretation
    • Declerck N., Machius M., Chambert R., Wiegand G., Huber R., Gaillardin C., Hyperthermostable mutants of Bacillus licheniformis α-amylase: thermodynamic studies and structural interpretation, Protein. Eng, 1997, 10, 541-549.
    • (1997) Protein. Eng , vol.10 , pp. 541-549
    • Declerck, N.1    Machius, M.2    Chambert, R.3    Wiegand, G.4    Huber, R.5    Gaillardin, C.6
  • 18
    • 0037837789 scopus 로고    scopus 로고
    • Kinetic stabilization of Bacillus licheniformis α-amylase through introduction of hydrophobic residues at the surface
    • Machius M., Declerck N., Huber R., Wiegand G., Kinetic stabilization of Bacillus licheniformis α-amylase through introduction of hydrophobic residues at the surface, J. Biol. Chem., 2003, 278, 11546-11553.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11546-11553
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 20
    • 27844479167 scopus 로고    scopus 로고
    • Thermostability of irreversible unfolding α-amylases analyzed by unfolding kinetics
    • Duy C., Fitter J., Thermostability of irreversible unfolding α-amylases analyzed by unfolding kinetics, J. Biol. Chem., 2005, 280, 37360-37365.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37360-37365
    • Duy, C.1    Fitter, J.2
  • 21
    • 0034717156 scopus 로고    scopus 로고
    • Stability and stabilization of globular proteins in solution
    • Jaenicke R., Stability and stabilization of globular proteins in solution, J. Biotechnol., 2000, 79, 193-203.
    • (2000) J. Biotechnol. , vol.79 , pp. 193-203
    • Jaenicke, R.1
  • 22
    • 0030220763 scopus 로고    scopus 로고
    • Engineering enzymes for stability
    • Shaw A., Bott R., Engineering enzymes for stability, Curr. Opin. Struct. Biol., 1996, 6, 546-550.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 546-550
    • Shaw, A.1    Bott, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.