메뉴 건너뛰기




Volumn 81, Issue 4, 2003, Pages 421-429

Bioimmobilization of keratinase using Bacillus subtilis and Escherichia coli systems

Author keywords

Fusion protein; Immobilization; Keratinase; Streptavidin

Indexed keywords

ESCHERICHIA COLI; GENETIC ENGINEERING; PROTEINS; PURIFICATION; SEPARATION;

EID: 0347297484     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10485     Document Type: Article
Times cited : (24)

References (51)
  • 2
    • 0030204090 scopus 로고    scopus 로고
    • Protein folding in vivo and renaturation of recombinant proteins from inclusion body
    • Andrew DG, West SM, Chaudhuri JB. 1996. Protein folding in vivo and renaturation of recombinant proteins from inclusion body. Mol Biotech 6:53-64.
    • (1996) Mol Biotech , vol.6 , pp. 53-64
    • Andrew, D.G.1    West, S.M.2    Chaudhuri, J.B.3
  • 4
    • 0001855568 scopus 로고    scopus 로고
    • In vivo folding of recombinant proteins in Escherichia coli
    • Atlas RM, Cohen G, Hershberger CL, Hu W-S, Sherman DH, Willson RC, editors. Washington, DC: ASM Press
    • nd ed. Washington, DC: ASM Press. p 551-565.
    • (1999) nd Ed , pp. 551-565
    • Baneyx, F.1
  • 5
    • 0024519918 scopus 로고
    • Postsecretory modifications of streptavidin
    • Bayer EA, Ben-Hur H, Wilchek M. 1989. Postsecretory modifications of streptavidin. Biochem J 259:369-376.
    • (1989) Biochem J , vol.259 , pp. 369-376
    • Bayer, E.A.1    Ben-Hur, H.2    Wilchek, M.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 7
    • 0242617623 scopus 로고
    • The properties of streptavidin, a biotin-binding protein produced by streptomyces
    • Chaiet L, Wolf FJ. 1964. The properties of streptavidin, a biotin-binding protein produced by streptomyces. Arch Biochem Biophys 106:1-5.
    • (1964) Arch Biochem Biophys , vol.106 , pp. 1-5
    • Chaiet, L.1    Wolf, F.J.2
  • 8
    • 0023504685 scopus 로고
    • Engineering for protein secretion in gram-positive bacteria
    • Chang S. 1987. Engineering for protein secretion in gram-positive bacteria. Meth Enzymol 153:507-516.
    • (1987) Meth Enzymol , vol.153 , pp. 507-516
    • Chang, S.1
  • 9
    • 84921072809 scopus 로고
    • Functional expression of human interferon genes and construction of a partition-proficient plasmid vector in B. subtilis
    • Ikeda Y, Beppu T, editors; Tokyo: Kodansha Ltd
    • Chang S, Ho D, Gray O, Chang SY, McLaughlin J. 1983. Functional expression of human interferon genes and construction of a partition-proficient plasmid vector in B. subtilis. In: Ikeda Y, Beppu T, editors. Genetics of industrial microbiology; Tokyo: Kodansha Ltd.
    • (1983) Genetics of Industrial Microbiology
    • Chang, S.1    Ho, D.2    Gray, O.3    Chang, S.Y.4    McLaughlin, J.5
  • 10
    • 0020180327 scopus 로고
    • Use of immobilized Streptomyces griseus protease (pronase) as a probe of structural transitions of lysozyme, β-lactoglobin and casein
    • Church FC, Catiagnani GL, Swaisgood HE. 1982. Use of immobilized Streptomyces griseus protease (pronase) as a probe of structural transitions of lysozyme, β-lactoglobin and casein. Enzyme Microb Technol 4:317-321.
    • (1982) Enzyme Microb Technol , vol.4 , pp. 317-321
    • Church, F.C.1    Catiagnani, G.L.2    Swaisgood, H.E.3
  • 11
    • 0022545127 scopus 로고
    • Potential use of Bacillus subtilis for secretion and production of foreign proteins
    • Doi RH, Wong S-L, Kawamura. F. 1984. Potential use of Bacillus subtilis for secretion and production of foreign proteins. Trends Biotechnol. 4:232-235.
    • (1984) Trends Biotechnol , vol.4 , pp. 232-235
    • Doi, R.H.1    Wong, S.-L.2    Kawamura, F.3
  • 12
    • 0003134029 scopus 로고
    • Isolation of Bacillus subtilis chromosomal DNA
    • Rodriquez RL, Trait RC, editors. Reading, MA: Addison-Wesley
    • Doi RH. 1983. Isolation of Bacillus subtilis chromosomal DNA. In Rodriquez RL, Trait RC, editors. Recombinant DNA techniques. Reading, MA: Addison-Wesley. p. 162-163.
    • (1983) Recombinant DNA Techniques , pp. 162-163
    • Doi, R.H.1
  • 13
    • 0026575440 scopus 로고
    • The autocatalytic processing of the subtilisin Carlsberg pro-region is independent of the primary structure of the cleavage site
    • Egnell P, Flock J. 1992. The autocatalytic processing of the subtilisin Carlsberg pro-region is independent of the primary structure of the cleavage site. Mol Microb 6:1115-1119.
    • (1992) Mol Microb , vol.6 , pp. 1115-1119
    • Egnell, P.1    Flock, J.2
  • 14
    • 0016415230 scopus 로고
    • Avidin
    • Anfinsen CB, Edsall JT, Richards, FM, editors. New York: Academic Press
    • Green, NM. 1975. Avidin. In Anfinsen CB, Edsall JT, Richards, FM, editors. Advances in protein chemistry, Vol. 29. New York: Academic Press. p. 82-133.
    • (1975) Advances in Protein Chemistry , vol.29 , pp. 82-133
    • Green, N.M.1
  • 15
    • 0023722280 scopus 로고
    • In vitro processing of prosubtilisin produced in Escherichia coli
    • Ikemura H, Inouye M. 1988. In vitro processing of prosubtilisin produced in Escherichia coli. J Biol Chem 263:12959-12963.
    • (1988) J Biol Chem , vol.263 , pp. 12959-12963
    • Ikemura, H.1    Inouye, M.2
  • 16
    • 0023644876 scopus 로고
    • Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli
    • Ikemura H, Takagi H, Inouye M. 1987. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. J Biol Chem 262:7859-7864.
    • (1987) J Biol Chem , vol.262 , pp. 7859-7864
    • Ikemura, H.1    Takagi, H.2    Inouye, M.3
  • 17
    • 0022429781 scopus 로고
    • Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis
    • Jacobs M, Eliasson M, Uhlen M, Flock JI. 1985. Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis. Nucleic Acids Res 13:8913-8922.
    • (1985) Nucleic Acids Res , vol.13 , pp. 8913-8922
    • Jacobs, M.1    Eliasson, M.2    Uhlen, M.3    Flock, J.I.4
  • 18
    • 0021193861 scopus 로고
    • Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neural protease
    • Kawamura F, Doi RH. 1984. Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neural protease. J Bacteriol 160:442-444.
    • (1984) J Bacteriol , vol.160 , pp. 442-444
    • Kawamura, F.1    Doi, R.H.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli K. 1970. Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, K.1
  • 21
    • 0032031269 scopus 로고    scopus 로고
    • Cloning and expression of a streptavidinlipase fusion gene in Escherichia coli and characterization of the immobilized fusion protein
    • Lee P, Swaisgood HE. 1998. Cloning and expression of a streptavidinlipase fusion gene in Escherichia coli and characterization of the immobilized fusion protein. Enzyme Microb Tech 22:246-254.
    • (1998) Enzyme Microb Tech , vol.22 , pp. 246-254
    • Lee, P.1    Swaisgood, H.E.2
  • 22
    • 0026795739 scopus 로고
    • Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain
    • Lin X, Lee CG, Casale ES, Shih JCH. 1992. Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain. Appl Env Microb 58:3271-3275.
    • (1992) Appl Env Microb , vol.58 , pp. 3271-3275
    • Lin, X.1    Lee, C.G.2    Casale, E.S.3    Shih, J.C.H.4
  • 23
    • 0029805302 scopus 로고    scopus 로고
    • Hydrolysis of feather keratin by immobilized keratinase
    • Lin X, Shih JCH, Swaisgood HE. 1996. Hydrolysis of feather keratin by immobilized keratinase. Appl Env Microb 62:4273-4275.
    • (1996) Appl Env Microb , vol.62 , pp. 4273-4275
    • Lin, X.1    Shih, J.C.H.2    Swaisgood, H.E.3
  • 24
    • 0030779256 scopus 로고    scopus 로고
    • Expression of the Bacillus licheniformis PWD-1 keratinase gene in B. subtilis
    • Lin X, Wong SL, Miller ES, Shih JCH. 1997. Expression of the Bacillus licheniformis PWD-1 keratinase gene in B. subtilis. J Ind Microb Biotech 19:134-138.
    • (1997) J Ind Microb Biotech , vol.19 , pp. 134-138
    • Lin, X.1    Wong, S.L.2    Miller, E.S.3    Shih, J.C.H.4
  • 25
    • 0028924379 scopus 로고
    • Nucleotide sequence and expression of kerA gene encoding a keratinolytic protease in Bacillus licheniformis PWD-1
    • Lin X., Kelemen DW, Miller ES, Shih JCH. 1995. Nucleotide sequence and expression of kerA gene encoding a keratinolytic protease in Bacillus licheniformis PWD-1. Appl Env Microb 61:1469-1474.
    • (1995) Appl Env Microb , vol.61 , pp. 1469-1474
    • Lin, X.1    Kelemen, D.W.2    Miller, E.S.3    Shih, J.C.H.4
  • 26
    • 0028326969 scopus 로고
    • Achievement of renaturation of subtilisin BPN' by a novel preceding using organic salts and digestible mutant of Streptomyces subtilisin inhibitor
    • Matsubara M, Kurimoto E, Kojima S, Miura K, Sakai T. 1994. Achievement of renaturation of subtilisin BPN' by a novel preceding using organic salts and digestible mutant of Streptomyces subtilisin inhibitor. FEBS Lett 342:193-196.
    • (1994) FEBS Lett , vol.342 , pp. 193-196
    • Matsubara, M.1    Kurimoto, E.2    Kojima, S.3    Miura, K.4    Sakai, T.5
  • 27
    • 0026168310 scopus 로고
    • Pro-peptide as an intramolecular chaperone: Renaturation of denatured subtilisin E with a synthetic pro-peptide
    • Ohta Y, Hojo H, Aimoto S, Kobayashi T, Zhu X, Jordan F, Inouye M. 1991. Pro-peptide as an intramolecular chaperone: Renaturation of denatured subtilisin E with a synthetic pro-peptide. Mol Microbiol 5:1507-1510.
    • (1991) Mol Microbiol , vol.5 , pp. 1507-1510
    • Ohta, Y.1    Hojo, H.2    Aimoto, S.3    Kobayashi, T.4    Zhu, X.5    Jordan, F.6    Inouye, M.7
  • 28
    • 0020438726 scopus 로고
    • Molecular cloning of α-amylase gene from Bacillus amyloliquefaciens and its expression in Bacillus subtilis
    • Palva I. 1982. Molecular cloning of α-amylase gene from Bacillus amyloliquefaciens and its expression in Bacillus subtilis. Gene 19:81-87.
    • (1982) Gene , vol.19 , pp. 81-87
    • Palva, I.1
  • 29
    • 0017652017 scopus 로고
    • Extracellular enzyme synthesis in the genus Bacillus
    • Priest FG. 1977. Extracellular enzyme synthesis in the genus Bacillus. Bacteriol Rev 41:711-753.
    • (1977) Bacteriol Rev , vol.41 , pp. 711-753
    • Priest, F.G.1
  • 32
    • 0025060796 scopus 로고
    • Expression of a streptavidin gene in Escherichia coli
    • Sano T, Cantor CR. 1990. Expression of a streptavidin gene in Escherichia coli. Proc Natl Acad Sci. USA 87:142-146.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 142-146
    • Sano, T.1    Cantor, C.R.2
  • 33
    • 0025857584 scopus 로고
    • Expression streptavidin-containing chimeric proteins
    • Sano T, Cantor CR. 1991. Expression streptavidin-containing chimeric proteins. Biochem Biophys Res Commun 176:571-577.
    • (1991) Biochem Biophys Res Commun , vol.176 , pp. 571-577
    • Sano, T.1    Cantor, C.R.2
  • 34
    • 0002864159 scopus 로고
    • Cell fractionation
    • Gerhardt P, Murray RGE, Wood WA, Krieg NR, editors. Washington, DC: American Society for Microbiology
    • Sprott GD, Koval SF, Schnaitman CA, 1994. Cell fractionation. In Gerhardt P, Murray RGE, Wood WA, Krieg NR, editors. Methods for general and molecular bacteriology. Washington, DC: American Society for Microbiology. p. 72-103.
    • (1994) Methods for General and Molecular Bacteriology , pp. 72-103
    • Sprott, G.D.1    Koval, S.F.2    Schnaitman, C.A.3
  • 35
    • 0031926846 scopus 로고    scopus 로고
    • Influence of a cell-wall-protease on production of α-amylase by Bacillus subtilis
    • Stephenson K, Harwoood CR. 1998. Influence of a cell-wall-protease on production of α-amylase by Bacillus subtilis. Appl Environ Microbiol 64:2875-2881.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2875-2881
    • Stephenson, K.1    Harwoood, C.R.2
  • 36
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studie FW, Moffatt BA. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189:113-130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studie, F.W.1    Moffatt, B.A.2
  • 38
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier FW. 1991. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J I Mol Biol 219:37-44.
    • (1991) J I Mol Biol , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 39
    • 0000737693 scopus 로고    scopus 로고
    • Inclusion bodies and refolding
    • Price N. editor. Oxford: BIOS Scientific
    • Thatcher DR, Wilks P, Chaudhuri JB. 1996. Inclusion bodies and refolding. In Price N. editor. Proteins labfax. Oxford: BIOS Scientific. p. 119-130.
    • (1996) Proteins Labfax , pp. 119-130
    • Thatcher, D.R.1    Wilks, P.2    Chaudhuri, J.B.3
  • 41
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheet: Procedure and some applications
    • Towbin HT, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheet: Procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.T.1    Staehelin, T.2    Gordon, J.3
  • 42
    • 0021127425 scopus 로고
    • Genes for alkaline proteases and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein
    • Vasantha N, Thompson LD, Rhodes G, Banner C, Nagle J, Filula D. 1984. Genes for alkaline proteases and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein. J Bacteriol 158: 811-819.
    • (1984) J Bacteriol , vol.158 , pp. 811-819
    • Vasantha, N.1    Thompson, L.D.2    Rhodes, G.3    Banner, C.4    Nagle, J.5    Filula, D.6
  • 43
    • 0030580110 scopus 로고    scopus 로고
    • Evidence for intramolecular processing of prosubtilisin sequestered on a solid support
    • Volkov A, Jordan F. 1996. Evidence for intramolecular processing of prosubtilisin sequestered on a solid support. J Mol Biol 262:595-599.
    • (1996) J Mol Biol , vol.262 , pp. 595-599
    • Volkov, A.1    Jordan, F.2
  • 44
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne G. 1990. The signal peptide. J Membr Biol 115:195-201.
    • (1990) J Membr Biol , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 45
    • 0028630399 scopus 로고
    • An Escherichia coli plasmid vector system for production of streptavidin fusion proteins: Expression and bioselective adsorption of streptavidin-β-galactosidase
    • Walsh MK, Swaisgood HE. 1994. An Escherichia coli plasmid vector system for production of streptavidin fusion proteins: expression and bioselective adsorption of streptavidin-β-galactosidase. Biotechnol Bioeng 44:1348-1354.
    • (1994) Biotechnol Bioeng , vol.44 , pp. 1348-1354
    • Walsh, M.K.1    Swaisgood, H.E.2
  • 46
    • 0032808211 scopus 로고    scopus 로고
    • Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB-29
    • Wang JJ, Shih JCH. 1999. Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB-29. J Ind Microb Biotech 22:608-616.
    • (1999) J Ind Microb Biotech , vol.22 , pp. 608-616
    • Wang, J.J.1    Shih, J.C.H.2
  • 47
    • 0023216607 scopus 로고
    • 43 operon of Bacillus subtilis
    • 43 operon of Bacillus subtilis. Mol Gen Genet 207:114-119.
    • (1987) Mol Gen Genet , vol.207 , pp. 114-119
    • Wang, L.F.1    Doi, R.H.2
  • 48
    • 0021112782 scopus 로고
    • Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis
    • Wells JA, Ferrari E, Henner DJ, Estell DA, Chen EY. 1983. Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis. Nucleic Acids Res 11:7911-7925.
    • (1983) Nucleic Acids Res , vol.11 , pp. 7911-7925
    • Wells, J.A.1    Ferrari, E.2    Henner, D.J.3    Estell, D.A.4    Chen, E.Y.5
  • 49
    • 84985059857 scopus 로고
    • Enumeration of some microbial groups in thermophilic poultry waste digesters and enrichment of a feather-degrading culture
    • Williams CM, Shih JCH. 1989. Enumeration of some microbial groups in thermophilic poultry waste digesters and enrichment of a feather-degrading culture. J App Bacterial 67:25-35.
    • (1989) J App Bacterial , vol.67 , pp. 25-35
    • Williams, C.M.1    Shih, J.C.H.2
  • 50
    • 0025301125 scopus 로고
    • Isolation, identification, and characterization of feather-degrading bacterium
    • Williams CM, Richter CS, Mackenzie JM, Shih JCH. 1990. Isolation, identification, and characterization of feather-degrading bacterium. Appl Env Microb 56:1509-1515.
    • (1990) Appl Env Microb , vol.56 , pp. 1509-1515
    • Williams, C.M.1    Richter, C.S.2    Mackenzie, J.M.3    Shih, J.C.H.4
  • 51
    • 0026338822 scopus 로고
    • Engineering a Bacillus subtilis expression-secretion system with a strain deficient in a six extracellular proteases
    • Wu XC, Lee W, Tran L, Wong SL. 1991. Engineering a Bacillus subtilis expression-secretion system with a strain deficient in a six extracellular proteases. J Bacteriol 173:4952-4958.
    • (1991) J Bacteriol , vol.173 , pp. 4952-4958
    • Wu, X.C.1    Lee, W.2    Tran, L.3    Wong, S.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.