메뉴 건너뛰기




Volumn 1, Issue 6, 2008, Pages 523-531

Directed evolution of Aspergillus niger glucoamylase to increase thermostability

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLUTAMINE; GLYCINE; HISTIDINE; LYSINE; SERINE; THREONINE; TYROSINE; VALINE;

EID: 77953596754     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2008.00055.x     Document Type: Article
Times cited : (14)

References (32)
  • 1
    • 0026726797 scopus 로고
    • Crystal structure of glucoamylase from Aspergillus awamori var X100 to 2.2-Å resolution
    • Aleshin, A.E., Golubev, A., Firsov, L.M., and Honzatko, R.B. (1992) Crystal structure of glucoamylase from Aspergillus awamori var X100 to 2.2-Å resolution. J Biol Chem 267: 19291-19298.
    • (1992) J Biol Chem , vol.267 , pp. 19291-19298
    • Aleshin, A.E.1    Golubev, A.2    Firsov, L.M.3    Honzatko, R.B.4
  • 2
    • 0028341842 scopus 로고
    • Refined crystal structures of glucoamylase from Aspergillus awamori var X100
    • Aleshin, A.E., Hoffman, C., Firsov, L.M., and Honzatko, R.B. (1994) Refined crystal structures of glucoamylase from Aspergillus awamori var X100. J Mol Biol 238: 575-591.
    • (1994) J Mol Biol , vol.238 , pp. 575-591
    • Aleshin, A.E.1    Hoffman, C.2    Firsov, L.M.3    Honzatko, R.B.4
  • 3
    • 0030056077 scopus 로고    scopus 로고
    • Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: Relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism
    • Aleshin, A.E., Stoffer, B., Firsov, L.M., Svenssopn, B., and Honzatko, R.B. (1996) Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism. Biochemistry 35: 8319-8328.
    • (1996) Biochemistry , vol.35 , pp. 8319-8328
    • Aleshin, A.E.1    Stoffer, B.2    Firsov, L.M.3    Svenssopn, B.4    Honzatko, R.B.5
  • 4
    • 0031695679 scopus 로고    scopus 로고
    • Stabilization of Aspergillus awamori glucoamylase by proline substitution and combining stabilizing mutations
    • Allen, M.J., Coutinho, P.M., and Ford, C.F. (1998) Stabilization of Aspergillus awamori glucoamylase by proline substitution and combining stabilizing mutations. Protein Eng 11: 783-788.
    • (1998) Protein Eng , vol.11 , pp. 783-788
    • Allen, M.J.1    Coutinho, P.M.2    Ford, C.F.3
  • 5
    • 0028764610 scopus 로고
    • Increased thermostability of Asn182Ala mutant glucoamylase
    • Chen, H.-M., Bakir, U., Reilly, P.J., and Ford, C. (1994) Increased thermostability of Asn182Ala mutant glucoamylase. Biotechnol Bioeng 43: 101-105.
    • (1994) Biotechnol Bioeng , vol.43 , pp. 101-105
    • Chen, H.-M.1    Bakir, U.2    Reilly, P.J.3    Ford, C.4
  • 6
    • 0029114490 scopus 로고
    • Identification and elimination by site-directed mutagenesis of thermolabile aspartyl bonds in Aspergillus awamori glucoamylase
    • Chen, H.-M., Ford, C.F., Reilly, P.J. (1995) Identification and elimination by site-directed mutagenesis of thermolabile aspartyl bonds in Aspergillus awamori glucoamylase. Protein Eng 8: 575-582.
    • (1995) Protein Eng , vol.8 , pp. 575-582
    • Chen, H.-M.1    Ford, C.F.2    Reilly, P.J.3
  • 7
    • 0029780410 scopus 로고    scopus 로고
    • Effect of replacing helical glycine residues with alanines on reversible and irreversible stability and production of Aspergillus awamori glucoamylase
    • Chen, H.-M., Li, Y., Panda, T., Buehler, F.U., Ford, C., and Reilly, P.J. (1996) Effect of replacing helical glycine residues with alanines on reversible and irreversible stability and production of Aspergillus awamori glucoamylase. Protein Eng 9: 499-505.
    • (1996) Protein Eng , vol.9 , pp. 499-505
    • Chen, H.-M.1    Li, Y.2    Panda, T.3    Buehler, F.U.4    Ford, C.5    Reilly, P.J.6
  • 9
    • 0033151659 scopus 로고    scopus 로고
    • Commodity scale production of sugars from starches
    • Crabb, W.D., and Shetty, J.K. (1999) Commodity scale production of sugars from starches. Curr Opin Microbiol 2: 252-256.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 252-256
    • Crabb, W.D.1    Shetty, J.K.2
  • 11
    • 0028145487 scopus 로고
    • Thermosensitive mutants of Aspergillus awamori glucoamylase by random mutagenesis: Inactivation kinetics and structural interpretation
    • Flory, N., Gorman, M., Coutinho, P.M., Ford, C., and Reilly, P.J. (1994) Thermosensitive mutants of Aspergillus awamori glucoamylase by random mutagenesis: inactivation kinetics and structural interpretation. Protein Eng 7: 1005-1012.
    • (1994) Protein Eng , vol.7 , pp. 1005-1012
    • Flory, N.1    Gorman, M.2    Coutinho, P.M.3    Ford, C.4    Reilly, P.J.5
  • 12
    • 0033179649 scopus 로고    scopus 로고
    • Improving operating performance of glucoamylase by mutagenesis
    • Ford, C. (1999) Improving operating performance of glucoamylase by mutagenesis. Curr Opin Biotechnol 10: 353-357.
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 353-357
    • Ford, C.1
  • 13
    • 0033578302 scopus 로고    scopus 로고
    • Cation-p interactions in structural biology
    • Gallivan, J.P., and Dougherty, D.A. (1999) Cation-p interactions in structural biology. Proc Natl Acad Sci USA 96: 9459-9464.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9459-9464
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 14
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phasespace distributions
    • Hoover,W.G. (1985) Canonical dynamics: equilibrium phasespace distributions. Phys Rev A 31: 1695-1697.
    • (1985) Phys Rev A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 15
  • 16
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen,W., Chandrasekhar, J., Madura, J., Impey, R., and Klein, M. (1983) Comparison of simple potential functions for simulating liquid water. J Chem Phys 79: 926-935.
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.1    Chandrasekhar, J.2    Madura, J.3    Impey, R.4    Klein, M.5
  • 17
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S., Tsai, C.J., and Nussinov, K. (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, K.3
  • 18
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung, D.W., Chen, E., and Goeddel, D.V. (1989) A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique 1: 11-15.
    • (1989) Technique , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 19
    • 0031468694 scopus 로고    scopus 로고
    • Effect of introducing disulfide bonds into Aspergillus awamori glucoamylase
    • Li, Y., Reilly, P.J., Ford, C.F. (1997) Effect of introducing disulfide bonds into Aspergillus awamori glucoamylase. Protein Eng 10: 1199-1204.
    • (1997) Protein Eng , vol.10 , pp. 1199-1204
    • Li, Y.1    Reilly, P.J.2    Ford, C.F.3
  • 20
    • 0031813816 scopus 로고    scopus 로고
    • Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase
    • Li, Y., Coutinho, P.M., and Ford, C. (1998) Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase. Protein Eng 11: 661-667.
    • (1998) Protein Eng , vol.11 , pp. 661-667
    • Li, Y.1    Coutinho, P.M.2    Ford, C.3
  • 21
    • 0037246131 scopus 로고    scopus 로고
    • Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations
    • Liu, H.-M., and Wang, W.-C. (2003) Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations. Protein Eng 16: 19-25.
    • (2003) Protein Eng , vol.16 , pp. 19-25
    • Liu, H.-M.1    Wang, W.-C.2
  • 22
    • 0041784950 scopus 로고    scopus 로고
    • All-Atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, J.A., Bashford, D., Bellot, M., Dunbrack, J.R., Evanseck, J., Field, M., et al. (1998) All-Atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102: 3586-3616.
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • MacKerell, J.A.1    Bashford, D.2    Bellot, M.3    Dunbrack, J.R.4    Evanseck, J.5    Field, M.6
  • 23
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad, D., Hunter, R., and Parker, R. (1992) A rapid method for localized mutagenesis of yeast genes. Yeast 8: 79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 24
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • Nosé, S. (1984) A unified formulation of the constant temperature molecular dynamics methods. J Chem Phys 81: 511-519.
    • (1984) J Chem Phys , vol.81 , pp. 511-519
    • Nosé, S.1
  • 27
    • 0000120116 scopus 로고    scopus 로고
    • Protein engineering of glucoamylase to improve industrial performance - a review
    • Reilly, P.J. (1999) Protein engineering of glucoamylase to improve industrial performance - a review. Starch/Stärke 51: 269-274.
    • (1999) Starch/Stärke , vol.51 , pp. 269-274
    • Reilly, P.J.1
  • 28
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a-helices
    • Richardson, J.S., and Richardson, D.C. (1988) Amino acid preferences for specific locations at the ends of a-helices. Science 240: 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 30
    • 0037032252 scopus 로고    scopus 로고
    • Comparisons of various types of hydrogen bonds involving aromatic amino acids
    • Scheiner, S., Karr, T., and Pattanayak, J. (2002) Comparisons of various types of hydrogen bonds involving aromatic amino acids. J Am Chem Soc 124: 13257-13264.
    • (2002) J Am Chem Soc , vol.124 , pp. 13257-13264
    • Scheiner, S.1    Karr, T.2    Pattanayak, J.3
  • 31
    • 0027434008 scopus 로고
    • Generation of temperature-sensitive cbp1 strains of Saccharomyces cerevisiae by PCR mutagenesis and in vivo recombination: Characteristics of the mutant strains imply that CBP1 is involved in stabilization and processing of cytochrome b Pre-mRNA
    • Staples, R.R., and Dieckmann, C.L. (1993) Generation of temperature-sensitive cbp1 strains of Saccharomyces cerevisiae by PCR mutagenesis and in vivo recombination: characteristics of the mutant strains imply that CBP1 is involved in stabilization and processing of cytochrome b Pre-mRNA. Genetics 135: 981-991.
    • (1993) Genetics , vol.135 , pp. 981-991
    • Staples, R.R.1    Dieckmann, C.L.2
  • 32
    • 33750147043 scopus 로고    scopus 로고
    • Improvement of Aspergillus niger glucoamylase thermostability by directed evolution
    • Wang, Y., Fuchs, E., Silva, R., McDaniel, A., Seibel, J., and Ford, C. (2006) Improvement of Aspergillus niger glucoamylase thermostability by directed evolution. Starch/ Stärke 58: 501-508.
    • (2006) Starch/ Stärke , vol.58 , pp. 501-508
    • Wang, Y.1    Fuchs, E.2    Silva, R.3    McDaniel, A.4    Seibel, J.5    Ford, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.