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Volumn 169, Issue 1, 2014, Pages 87-94

Insights on activity and stability of subtilisin E towards guanidinium chloride and sodium dodecylsulfate

Author keywords

Chaotolerance; Directed evolution; Guanidinium chloride; Protease; SDS

Indexed keywords

CHAOTOLERANCE; DIRECTED EVOLUTION; GUANIDINIUM CHLORIDES; PROTEASE; SDS;

EID: 84889562616     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.11.001     Document Type: Article
Times cited : (10)

References (28)
  • 1
    • 0035807040 scopus 로고    scopus 로고
    • Cation-dependent stability of subtilisin
    • Alexander P.A., Ruan B., Bryan P.N. Cation-dependent stability of subtilisin. Biochemistry 2001, 40:10634-10639.
    • (2001) Biochemistry , vol.40 , pp. 10634-10639
    • Alexander, P.A.1    Ruan, B.2    Bryan, P.N.3
  • 2
    • 0033578390 scopus 로고    scopus 로고
    • Selection for improved subtiligases by phage display
    • Atwell S., Wells J.A. Selection for improved subtiligases by phage display. PNAS 1999, 96:9497-9502.
    • (1999) PNAS , vol.96 , pp. 9497-9502
    • Atwell, S.1    Wells, J.A.2
  • 4
    • 0023181650 scopus 로고
    • Rapid isolation of eukaryotic DNA
    • Bowtell D.D. Rapid isolation of eukaryotic DNA. Anal. Biochem. 1987, 162:463-465.
    • (1987) Anal. Biochem. , vol.162 , pp. 463-465
    • Bowtell, D.D.1
  • 5
    • 0034731382 scopus 로고    scopus 로고
    • Protein engineering of subtilisin
    • Bryan P.N. Protein engineering of subtilisin. Biochim. Biophys. Acta 2000, 1543:203-222.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 203-222
    • Bryan, P.N.1
  • 7
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
    • Chen K., Arnold F.H. Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. PNAS 1993, 90:5618-5622.
    • (1993) PNAS , vol.90 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 8
    • 0026124848 scopus 로고
    • Enzyme engineering for nonaqueous solvents. II. Additive effects of mutations on the stability and activity of subtilisin E in polar organic media
    • Chen K.Q., Robinson A.C., Van Dam M.E., Martinez P., Economou C., Arnold F.H. Enzyme engineering for nonaqueous solvents. II. Additive effects of mutations on the stability and activity of subtilisin E in polar organic media. Biotechnol. Progr. 1991, 7:125-129.
    • (1991) Biotechnol. Progr. , vol.7 , pp. 125-129
    • Chen, K.Q.1    Robinson, A.C.2    Van Dam, M.E.3    Martinez, P.4    Economou, C.5    Arnold, F.H.6
  • 9
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin J.M., Przybyla A.E., MacDonald R.J., Rutter W.J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 1979, 18:5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 1987, 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 11
    • 0025179832 scopus 로고
    • Protein folding
    • Creighton T.E. Protein folding. Biochem. J. 1990, 270:1-16.
    • (1990) Biochem. J. , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 13
    • 0016794680 scopus 로고
    • Stimulation of proteinase K action by denaturing agents: application to the isolation of nucleic acids and the degradation of 'masked' proteins
    • Hilz H., Wiegers U., Adamietz P. Stimulation of proteinase K action by denaturing agents: application to the isolation of nucleic acids and the degradation of 'masked' proteins. Eur. J. Biochem. 1975, 56:103-108.
    • (1975) Eur. J. Biochem. , vol.56 , pp. 103-108
    • Hilz, H.1    Wiegers, U.2    Adamietz, P.3
  • 15
    • 84863351785 scopus 로고    scopus 로고
    • Directed evolution of subtilisin E into a highly active and guanidinium chloride- and sodium dodecylsulfate-tolerant protease
    • Li Z., Roccatano D., Lorenz M., Schwaneberg U. Directed evolution of subtilisin E into a highly active and guanidinium chloride- and sodium dodecylsulfate-tolerant protease. ChemBioChem 2012, 13:691-699.
    • (2012) ChemBioChem , vol.13 , pp. 691-699
    • Li, Z.1    Roccatano, D.2    Lorenz, M.3    Schwaneberg, U.4
  • 16
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: proteins with a grain of salt
    • Mevarech M., Frolow F., Gloss L.M. Halophilic enzymes: proteins with a grain of salt. Biophys. Chem. 2000, 86:155-164.
    • (2000) Biophys. Chem. , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 18
    • 0026710554 scopus 로고
    • Protein structures in SDS micelle-protein complexes
    • Parker W., Song P.S. Protein structures in SDS micelle-protein complexes. Biophys. J. 1992, 61:1435-1439.
    • (1992) Biophys. J. , vol.61 , pp. 1435-1439
    • Parker, W.1    Song, P.S.2
  • 19
    • 33745182284 scopus 로고    scopus 로고
    • 2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: the propeptide is a potent inhibitor of the mature domain but is not required for its folding
    • 2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: the propeptide is a potent inhibitor of the mature domain but is not required for its folding. Appl. Environ. Microbiol. 2006, 72:4154-4162.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4154-4162
    • Pulido, M.1    Saito, K.2    Tanaka, S.3    Koga, Y.4    Morikawa, M.5    Takano, K.6    Kanaya, S.7
  • 20
    • 0019877658 scopus 로고
    • Structural stability of halophilic proteins
    • Rao J.K., Argos P. Structural stability of halophilic proteins. Biochemistry 1981, 20:6536-6543.
    • (1981) Biochemistry , vol.20 , pp. 6536-6543
    • Rao, J.K.1    Argos, P.2
  • 22
    • 33846613819 scopus 로고    scopus 로고
    • Activity of subtilisin carlsberg in macromolecular crowding
    • Shaw A.K., Pal S.K. Activity of subtilisin carlsberg in macromolecular crowding. J. Photochem. Photobiol., B 2007, 86:199-206.
    • (2007) J. Photochem. Photobiol., B , vol.86 , pp. 199-206
    • Shaw, A.K.1    Pal, S.K.2
  • 23
    • 72549111666 scopus 로고    scopus 로고
    • Inhibition kinetics and the aggregation of alpha-glucosidase by different denaturants
    • Wu X.Q., Xu H., Yue H., Liu K.Q., Wang X.Y. Inhibition kinetics and the aggregation of alpha-glucosidase by different denaturants. Protein J. 2009, 28:448-456.
    • (2009) Protein J. , vol.28 , pp. 448-456
    • Wu, X.Q.1    Xu, H.2    Yue, H.3    Liu, K.Q.4    Wang, X.Y.5
  • 24
    • 0029969577 scopus 로고    scopus 로고
    • Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
    • You L., Arnold F.H. Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide. Protein Eng. 1996, 9:77-83.
    • (1996) Protein Eng. , vol.9 , pp. 77-83
    • You, L.1    Arnold, F.H.2
  • 25
    • 0030858562 scopus 로고    scopus 로고
    • Functional and nonfunctional mutations distinguished by random recombination of homologous genes
    • Zhao H., Arnold F.H. Functional and nonfunctional mutations distinguished by random recombination of homologous genes. PNAS 1997, 94:7997-8000.
    • (1997) PNAS , vol.94 , pp. 7997-8000
    • Zhao, H.1    Arnold, F.H.2
  • 26
    • 0032973026 scopus 로고    scopus 로고
    • Directed evolution converts subtilisin E into a functional equivalent of thermitase
    • Zhao H.M., Arnold F.H. Directed evolution converts subtilisin E into a functional equivalent of thermitase. Protein Eng. 1999, 12:47-53.
    • (1999) Protein Eng. , vol.12 , pp. 47-53
    • Zhao, H.M.1    Arnold, F.H.2
  • 27
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step site-directed and site-saturation mutagenesis protocol
    • Zheng L., Baumann U., Reymond J.L. An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res. 2004, 32:e115.
    • (2004) Nucleic Acids Res. , vol.32
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3
  • 28
    • 0030625879 scopus 로고    scopus 로고
    • Protein engineering on subtilisin E
    • Zhu L., Ji Y. Protein engineering on subtilisin E. Chin. J. Biotechnol. 1997, 13:9-15.
    • (1997) Chin. J. Biotechnol. , vol.13 , pp. 9-15
    • Zhu, L.1    Ji, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.