메뉴 건너뛰기




Volumn 75, Issue 16, 2009, Pages 5424-5427

Alleviation of proteolytic sensitivity to enhance recombinant lipase production in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ANTARCTICA; CO-EXPRESSION; DOUBLE MUTANTS; FUNCTIONAL EXPRESSION; LIPASE PRODUCTION; MISFOLDING; RECOMBINANT PROTEIN PRODUCTIONS;

EID: 68549106132     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00740-09     Document Type: Article
Times cited : (19)

References (22)
  • 1
    • 0031795317 scopus 로고    scopus 로고
    • One biocatalyst-many applications: The use of Candida antarctica lipase B in organic synthesis
    • Anderson, E. M., K. M. Larsson, and O. Kirk. 1998. One biocatalyst-many applications: the use of Candida antarctica lipase B in organic synthesis. Biocatal. Biotransform. 16:181-204.
    • (1998) Biocatal. Biotransform , vol.16 , pp. 181-204
    • Anderson, E.M.1    Larsson, K.M.2    Kirk, O.3
  • 2
    • 0024536385 scopus 로고
    • Identification of C-terminal extensions that protect proteins from intracellular proteolysis
    • Bowie, J. U., and R. T. Sauer. 1989. Identification of C-terminal extensions that protect proteins from intracellular proteolysis. J. Biol. Chem. 264:7596-7602.
    • (1989) J. Biol. Chem , vol.264 , pp. 7596-7602
    • Bowie, J.U.1    Sauer, R.T.2
  • 3
    • 0000671329 scopus 로고
    • Low temperatures stabilize interferon a-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli
    • Chesshyre, J. A., and A. R. Hipkiss. 1989. Low temperatures stabilize interferon a-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli. Appl. Microbiol. Biotechnol. 31:158-162.
    • (1989) Appl. Microbiol. Biotechnol , vol.31 , pp. 158-162
    • Chesshyre, J.A.1    Hipkiss, A.R.2
  • 4
    • 0003475771 scopus 로고
    • The selective degradation of abnormal proteins in bacteria
    • W. R. Gold ed, Butterworths, Boston, MA
    • Goldberg, A. L., and S. A. Goff. 1986. The selective degradation of abnormal proteins in bacteria, p. 287-314. In W. R. Gold (ed.), Maximizing gene expression. Butterworths, Boston, MA.
    • (1986) Maximizing gene expression , pp. 287-314
    • Goldberg, A.L.1    Goff, S.A.2
  • 5
    • 0025353947 scopus 로고
    • Minimizing proteolysis in Escherichia coli: Genetic solutions
    • Gottesman, S. 1990. Minimizing proteolysis in Escherichia coli: genetic solutions. Methods Enzymol. 185:119-129.
    • (1990) Methods Enzymol , vol.185 , pp. 119-129
    • Gottesman, S.1
  • 6
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman, S. 1996. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:465-506.
    • (1996) Annu. Rev. Genet , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 7
    • 0026454716 scopus 로고
    • Regulation by proteolysis: Energydependent proteases and their targets
    • Gottesman, S., and M. R. Maurizi. 1992. Regulation by proteolysis: energydependent proteases and their targets. Microbiol. Rev. 56:592-621.
    • (1992) Microbiol. Rev , vol.56 , pp. 592-621
    • Gottesman, S.1    Maurizi, M.R.2
  • 9
    • 0026601663 scopus 로고
    • Proteases and protein degradation in Escherichia coli
    • Maurizi, M. R. 1992. Proteases and protein degradation in Escherichia coli. Experientia 48:178-201.
    • (1992) Experientia , vol.48 , pp. 178-201
    • Maurizi, M.R.1
  • 10
    • 0028143313 scopus 로고
    • Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins
    • Meerman, H. J., and G. Georgoiu. 1994. Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins. Bio/Technology 12:1107-1110.
    • (1994) Bio/Technology , vol.12 , pp. 1107-1110
    • Meerman, H.J.1    Georgoiu, G.2
  • 11
    • 0029025537 scopus 로고
    • Hydrophobicity engineering to increase solubility and stability of a recombinant protein from respiratory syncytial virus
    • Murby, M., E. Samuelsson, T. N. Nguyen, L. Mignard, U. Power, H. Binz, M. Uhlen, and S. Stahl. 1995. Hydrophobicity engineering to increase solubility and stability of a recombinant protein from respiratory syncytial virus. Eur. J. Biochem. 230:38-44.
    • (1995) Eur. J. Biochem , vol.230 , pp. 38-44
    • Murby, M.1    Samuelsson, E.2    Nguyen, T.N.3    Mignard, L.4    Power, U.5    Binz, H.6    Uhlen, M.7    Stahl, S.8
  • 13
    • 0343196676 scopus 로고    scopus 로고
    • Effect of mutation in non-consensus sequence Thr-X-Ser-X-Gly of Candida antarctica lipase B on lipase specificity, specific activity and thermostability
    • Patkar, S. A., A. Svendsen, O. Kirk, I. G. Clausen, and K. Borch. 1997. Effect of mutation in non-consensus sequence Thr-X-Ser-X-Gly of Candida antarctica lipase B on lipase specificity, specific activity and thermostability. J. Mol. Catal. B Enzymol. 3:51-54.
    • (1997) J. Mol. Catal. B Enzymol , vol.3 , pp. 51-54
    • Patkar, S.A.1    Svendsen, A.2    Kirk, O.3    Clausen, I.G.4    Borch, K.5
  • 14
    • 0035496145 scopus 로고    scopus 로고
    • Improved enantioselectivity of a lipase by rational protein engineering
    • Rotticci, D., J. C. Rotticci-Mulder, S. Denman, T. Norin, and K. Hult. 2001. Improved enantioselectivity of a lipase by rational protein engineering. ChemBioChem 2:766-770.
    • (2001) ChemBioChem , vol.2 , pp. 766-770
    • Rotticci, D.1    Rotticci-Mulder, J.C.2    Denman, S.3    Norin, T.4    Hult, K.5
  • 15
    • 0842331856 scopus 로고    scopus 로고
    • N-terminal truncation circumvents proteolytic degradation of the human HtrA2/Omi serine protease in Escherichia coli: Rapid purification of a proteolytically active HtrA2/Omi
    • Seong, Y. M., H. J. Park, G. H. Seong, J. Y. Choi, S. J. K. Yoon, B. R. Min, S. M. Kang, and H. S. Rhim. 2004. N-terminal truncation circumvents proteolytic degradation of the human HtrA2/Omi serine protease in Escherichia coli: rapid purification of a proteolytically active HtrA2/Omi. Protein Expr. Purif. 33:200-208.
    • (2004) Protein Expr. Purif , vol.33 , pp. 200-208
    • Seong, Y.M.1    Park, H.J.2    Seong, G.H.3    Choi, J.Y.4    Yoon, S.J.K.5    Min, B.R.6    Kang, S.M.7    Rhim, H.S.8
  • 16
    • 1842765645 scopus 로고    scopus 로고
    • Improved activity and thermostability of Candida antarctica lipase B by DNA family shuffling
    • Suen, W. C., N. Zhang, L. Xiao, V. Madison, and A. Zaks. 2004. Improved activity and thermostability of Candida antarctica lipase B by DNA family shuffling. Protein Eng. Des. Sel. 17:133-140.
    • (2004) Protein Eng. Des. Sel , vol.17 , pp. 133-140
    • Suen, W.C.1    Zhang, N.2    Xiao, L.3    Madison, V.4    Zaks, A.5
  • 17
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • Uppenberg, J., M. T. Hansen, S. Patkar, and T. A. Jones. 1994. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure 2:293-308.
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 18
    • 0031798531 scopus 로고    scopus 로고
    • Role of paired basic residues in the expression of active recombinant galactosyltransferases from the bacterial pathogen Neisseria meningitidis
    • Wakarchuk, W. W., A. Cunningham, D. C. Watson, and N. M. Young. 1998. Role of paired basic residues in the expression of active recombinant galactosyltransferases from the bacterial pathogen Neisseria meningitidis. Protein Eng. 11:295-302.
    • (1998) Protein Eng , vol.11 , pp. 295-302
    • Wakarchuk, W.W.1    Cunningham, A.2    Watson, D.C.3    Young, N.M.4
  • 19
    • 0028819842 scopus 로고
    • Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli
    • Wall, J. G., and A. Pluckthun. 1995. Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6:507-516.
    • (1995) Curr. Opin. Biotechnol , vol.6 , pp. 507-516
    • Wall, J.G.1    Pluckthun, A.2
  • 20
    • 46149108793 scopus 로고    scopus 로고
    • Effect of folding factors in rescuing unstable heterologous lipase B to enhance its overexpression in the periplasm of Escherichia coli
    • Xu, Y., D. Lewis, and C. P. Chou. 2008. Effect of folding factors in rescuing unstable heterologous lipase B to enhance its overexpression in the periplasm of Escherichia coli. Appl. Microbiol. Biotechnol. 79:1035-1044.
    • (2008) Appl. Microbiol. Biotechnol , vol.79 , pp. 1035-1044
    • Xu, Y.1    Lewis, D.2    Chou, C.P.3
  • 21
    • 54349105625 scopus 로고    scopus 로고
    • Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation
    • Xu, Y., A. Yasin, R. Tang, J. M. Scharer, M. Moo-Young, and C. P. Chou. 2008. Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation. Appl. Microbiol. Biotechnol. 81:79-87.
    • (2008) Appl. Microbiol. Biotechnol , vol.81 , pp. 79-87
    • Xu, Y.1    Yasin, A.2    Tang, R.3    Scharer, J.M.4    Moo-Young, M.5    Chou, C.P.6
  • 22
    • 54849424929 scopus 로고    scopus 로고
    • Enhancing functional expression of heterologous lipase in the periplasm of Escherichia coli
    • Xu, Y., A. Yasin, T. Wucherpfennig, and C. P. Chou. 2008. Enhancing functional expression of heterologous lipase in the periplasm of Escherichia coli. World J. Microbiol. Biotechnol. 12:2827-2835.
    • (2008) World J. Microbiol. Biotechnol , vol.12 , pp. 2827-2835
    • Xu, Y.1    Yasin, A.2    Wucherpfennig, T.3    Chou, C.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.