메뉴 건너뛰기




Volumn 60, Issue 5, 1998, Pages 608-616

Site-directed and random immobilization of subtilisin on functionalized membranes: Activity determination in aqueous and organic media

Author keywords

Membrane; Oriented immobilization; Site directed mutagenesis; Subtilisin

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; ENZYME KINETICS; HYDROPHOBICITY; MICROFILTRATION; MUTAGENESIS; ORGANIC SOLVENTS; POLYMERIC MEMBRANES; POLYSULFONES;

EID: 0032488339     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19981205)60:5<608::AID-BIT11>3.0.CO;2-Q     Document Type: Article
Times cited : (43)

References (33)
  • 1
    • 0025757012 scopus 로고
    • Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution
    • Abrahmsen, L., Tom, J., Burnier, J., Butcher, K. A., Kossiakoff, A., Wells, J. A. 1991. Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution. Biochemistry 30: 4151-4159.
    • (1991) Biochemistry , vol.30 , pp. 4151-4159
    • Abrahmsen, L.1    Tom, J.2    Burnier, J.3    Butcher, K.A.4    Kossiakoff, A.5    Wells, J.A.6
  • 2
    • 0026763422 scopus 로고
    • Solvent dielectric effects on protein dynamics
    • U.S.A.
    • Affleck, R., Haynes, C. A., Clark, D. S. 1992. Solvent dielectric effects on protein dynamics. Proc. Natl. Acad. Sci. U.S.A. 89: 5167-5170.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 5167-5170
    • Affleck, R.1    Haynes, C.A.2    Clark, D.S.3
  • 3
    • 0025485121 scopus 로고
    • Engineering enzymes for non-aqueous solvents
    • Arnold, F. H. 1990. Engineering enzymes for non-aqueous solvents. Trends Biotechnol. 8: 244-249.
    • (1990) Trends Biotechnol. , vol.8 , pp. 244-249
    • Arnold, F.H.1
  • 4
    • 0344695054 scopus 로고
    • Engineering altered substrate specificity into subtilisin BPN'
    • D. Kamely. A. M. Chakrabarty, and S. E. Kornguth (eds.), Kluwer Academic Publishers, Boston
    • Bott, R., Graycar, T., Estell, D. 1991. Engineering altered substrate specificity into subtilisin BPN', pp. 429-440. In: D. Kamely. A. M. Chakrabarty, and S. E. Kornguth (eds.), Biotechnology. Kluwer Academic Publishers, Boston.
    • (1991) Biotechnology , pp. 429-440
    • Bott, R.1    Graycar, T.2    Estell, D.3
  • 5
    • 0024278654 scopus 로고
    • The three-dimensional structure of Bacillus amyloliquefaciens subtilisin at 1.8 Å and an analysis of the structural consequences of peroxide inactivation
    • Bott, R., Ultsch, M., Kossiakoff, A., Graycar, T., Katz, B., Power, S. 1988. The three-dimensional structure of Bacillus amyloliquefaciens subtilisin at 1.8 Å and an analysis of the structural consequences of peroxide inactivation. J. Biol. Chem. 263: 7895-7906.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7895-7906
    • Bott, R.1    Ultsch, M.2    Kossiakoff, A.3    Graycar, T.4    Katz, B.5    Power, S.6
  • 6
    • 0004039284 scopus 로고
    • Academic Press, New York
    • Boyer, P. D. 1971. The Enzymes, Vol. III. Academic Press, New York.
    • (1971) The Enzymes , vol.3
    • Boyer, P.D.1
  • 7
    • 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
  • 9
    • 0025499795 scopus 로고
    • Principles of biological membrane structure: Alterations in the physical state of one side of the membrane by modulation of the physical state of the opposite side
    • Butterfield, D. A. 1990. Principles of biological membrane structure: Alterations in the physical state of one side of the membrane by modulation of the physical state of the opposite side. J. Membr. Sci. 53: 3-17.
    • (1990) J. Membr. Sci. , vol.53 , pp. 3-17
    • Butterfield, D.A.1
  • 11
    • 0030709602 scopus 로고    scopus 로고
    • Biofunctional membranes: Electron paramagnetic resonance studies of the active site structure of enzymes site-specifically immobilized onto polymeric supports through molecular recognition
    • Butterfield, D. A., Subramaniam, R., Bhattacharyya, D., Viswanath, S., Huang, W., Bachas, L. G. 1997. Biofunctional membranes: Electron paramagnetic resonance studies of the active site structure of enzymes site-specifically immobilized onto polymeric supports through molecular recognition. Polym. Mater. Sci. Eng. Preprints 76: 602-603.
    • (1997) Polym. Mater. Sci. Eng. Preprints , vol.76 , pp. 602-603
    • Butterfield, D.A.1    Subramaniam, R.2    Bhattacharyya, D.3    Viswanath, S.4    Huang, W.5    Bachas, L.G.6
  • 12
    • 0016623368 scopus 로고
    • Some properties of a protease (subtilisin BPN') immobilized to porous glass
    • Chapman, J. D., Hultin, H. O. 1975. Some properties of a protease (subtilisin BPN') immobilized to porous glass. Biotechnol. Bioeng. 17: 1783-1795.
    • (1975) Biotechnol. Bioeng. , vol.17 , pp. 1783-1795
    • Chapman, J.D.1    Hultin, H.O.2
  • 13
    • 0021830125 scopus 로고
    • Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation
    • Estell, D. A., Graycar, T. P., Wells, J. A. 1985. Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation. J. Biol. Chem. 260: 6518-6521.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6518-6521
    • Estell, D.A.1    Graycar, T.P.2    Wells, J.A.3
  • 14
    • 0029379907 scopus 로고
    • Flat sheet and hollow fiber membrane bioreactors: A study of kinetics and active site conformational changes of immobilized papain including sorption studies of reaction constituents
    • Ganapathi, S., Butterfield, D. A., Bhattacharyya, D. 1995. Flat sheet and hollow fiber membrane bioreactors: A study of kinetics and active site conformational changes of immobilized papain including sorption studies of reaction constituents. J. Chem. Technol. Biotechnol. 64: 157-164.
    • (1995) J. Chem. Technol. Biotechnol. , vol.64 , pp. 157-164
    • Ganapathi, S.1    Butterfield, D.A.2    Bhattacharyya, D.3
  • 15
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous-organic mixtures but not in pure organic solvents
    • Griebenow, K., Klibanov, A. 1996. On protein denaturation in aqueous-organic mixtures but not in pure organic solvents. J. Am. Chem. Soc. 118: 11695-11700.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11695-11700
    • Griebenow, K.1    Klibanov, A.2
  • 16
    • 0026112863 scopus 로고
    • Activity and flexibility of alcohol dehydrogenase in organic solvents
    • Guinn, M., Skerker, P., Kavanaugh, P., Clark, D. 1991. Activity and flexibility of alcohol dehydrogenase in organic solvents. Biotechnol. Bioeng. 37: 303-308.
    • (1991) Biotechnol. Bioeng. , vol.37 , pp. 303-308
    • Guinn, M.1    Skerker, P.2    Kavanaugh, P.3    Clark, D.4
  • 18
    • 0031573245 scopus 로고    scopus 로고
    • Improving the activity of immobilized subtilisin by site-specific attachment to surfaces
    • Huang, W., Wang, J., Bhattacharyya, D., Bachas, L. G. 1997. Improving the activity of immobilized subtilisin by site-specific attachment to surfaces. Anal. Chem. 69: 4601-4607.
    • (1997) Anal. Chem. , vol.69 , pp. 4601-4607
    • Huang, W.1    Wang, J.2    Bhattacharyya, D.3    Bachas, L.G.4
  • 19
    • 0028567450 scopus 로고
    • Effect of support material and enzyme pretreatment on enantioselectivity of immobilized subtilisin in organic solvents
    • Orsat, B., Drtina, G., Williams, M., Klibanov, A. 1994. Effect of support material and enzyme pretreatment on enantioselectivity of immobilized subtilisin in organic solvents. Biotechnol. Bioeng. 44: 1265-1269.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 1265-1269
    • Orsat, B.1    Drtina, G.2    Williams, M.3    Klibanov, A.4
  • 21
    • 0028437059 scopus 로고
    • Solvation of CBZ-amino acid nitrophenyl esters in organic media and the kinetics of their transesterification by subtilisin
    • Reimann, A., Robb, D. A., Hailing, P. J. 1994. Solvation of CBZ-amino acid nitrophenyl esters in organic media and the kinetics of their transesterification by subtilisin. Biotech. Bioeng. 43: 1081-1086.
    • (1994) Biotech. Bioeng. , vol.43 , pp. 1081-1086
    • Reimann, A.1    Robb, D.A.2    Hailing, P.J.3
  • 22
    • 0024287153 scopus 로고
    • On the importance of support material for bioorganic synthesis
    • Reslow, M., Adlercreutz, P., Mattiasson, B. 1988. On the importance of support material for bioorganic synthesis. Eur. J. Biocbem. 172: 573-578.
    • (1988) Eur. J. Biocbem. , vol.172 , pp. 573-578
    • Reslow, M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 23
    • 0027442363 scopus 로고
    • An engineered disulfide cross-link accelerates the refolding rate of calcium-free subtilisin by 850-fold
    • Strausberg, S., Alexander, P., Wand, L., Gallagher, T., Gilliland, G., Bryan, P. 1993. An engineered disulfide cross-link accelerates the refolding rate of calcium-free subtilisin by 850-fold. Biochemistry 32: 10371-10377.
    • (1993) Biochemistry , vol.32 , pp. 10371-10377
    • Strausberg, S.1    Alexander, P.2    Wand, L.3    Gallagher, T.4    Gilliland, G.5    Bryan, P.6
  • 24
    • 0345125747 scopus 로고    scopus 로고
    • Structure-activity correlation of subtilisin immobilized on modified poly(ether)sulfone membrane by covalent and non-covalent linkages
    • D. A. Butterfield (ed.), Plenum Press, New York
    • Subramaniam, R., Butterfield, D. A. 1996. Structure-activity correlation of subtilisin immobilized on modified poly(ether)sulfone membrane by covalent and non-covalent linkages, pp. 201-208. In: D. A. Butterfield (ed.), Biofunctional Membranes. Plenum Press, New York.
    • (1996) Biofunctional Membranes , pp. 201-208
    • Subramaniam, R.1    Butterfield, D.A.2
  • 25
    • 0025232324 scopus 로고
    • Enhancement of the thermostability of subtilisin e by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease
    • Takagi, H., Takahashi, T., Momose, H., Inouye, M., Maeda, Y., Matsuzawa, H., Ohta, T. 1990. Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease. J. Biol. Chem. 265: 6874-6878.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6874-6878
    • Takagi, H.1    Takahashi, T.2    Momose, H.3    Inouye, M.4    Maeda, Y.5    Matsuzawa, H.6    Ohta, T.7
  • 26
    • 0000054517 scopus 로고
    • Rotational diffusion studied by passage saturation transfer electron paramagnetic resonance
    • Thomas, D. D., Dalton, L. R., Hyde, J. S. 1976. Rotational diffusion studied by passage saturation transfer electron paramagnetic resonance. J. Chem. Phys. 65: 3006-3024.
    • (1976) J. Chem. Phys. , vol.65 , pp. 3006-3024
    • Thomas, D.D.1    Dalton, L.R.2    Hyde, J.S.3
  • 27
    • 0022386437 scopus 로고
    • Tailoring the pH dependence of enzyme catalysis using protein engineering
    • Thomas, P. G., Russell, A. J., Fersht, A. R. 1985. Tailoring the pH dependence of enzyme catalysis using protein engineering. Nature 318: 375-376.
    • (1985) Nature , vol.318 , pp. 375-376
    • Thomas, P.G.1    Russell, A.J.2    Fersht, A.R.3
  • 28
    • 0028904921 scopus 로고
    • The properties of subtilisin, Novo type, immobilized on porous glass
    • Trzmiel, T., Fortak, M., Galas, E. 1995. The properties of subtilisin, Novo type, immobilized on porous glass. Acta Biotechnol. 15: 123-129.
    • (1995) Acta Biotechnol. , vol.15 , pp. 123-129
    • Trzmiel, T.1    Fortak, M.2    Galas, E.3
  • 29
    • 0028282678 scopus 로고
    • Relationship between water activity and catalytic activity of lipases in organic media
    • Valivety, R. H., Halling, P. J., Peilow, A. D., Macrae, A. R. 1994. Relationship between water activity and catalytic activity of lipases in organic media. Eur J. Biochem. 222: 461-466.
    • (1994) Eur J. Biochem. , vol.222 , pp. 461-466
    • Valivety, R.H.1    Halling, P.J.2    Peilow, A.D.3    Macrae, A.R.4
  • 30
    • 0028874414 scopus 로고
    • Site-directed and random immobilization on functionalized membranes: Kinetic studies and models
    • Vishwanath, S., Bhattacharyya, D., Huang, W., Bachas, L. G. 1995. Site-directed and random immobilization on functionalized membranes: Kinetic studies and models. J. Membr. Sci. 108: 1-13.
    • (1995) J. Membr. Sci. , vol.108 , pp. 1-13
    • Vishwanath, S.1    Bhattacharyya, D.2    Huang, W.3    Bachas, L.G.4
  • 31
    • 0031105299 scopus 로고    scopus 로고
    • Kinetic studies of site-specifically and randomly immobilized alkaline phosphatase on functionalized membranes
    • Vishwanath, S., Watson, C. R., Huang, W., Bachas, L. G., Bhattacharyya, D. 1997. Kinetic studies of site-specifically and randomly immobilized alkaline phosphatase on functionalized membranes. J. Chem. Technol. Biotechnol. 68: 294-302.
    • (1997) J. Chem. Technol. Biotechnol. , vol.68 , pp. 294-302
    • Vishwanath, S.1    Watson, C.R.2    Huang, W.3    Bachas, L.G.4    Bhattacharyya, D.5
  • 32
    • 0031047280 scopus 로고    scopus 로고
    • Structure and function of subtilisin BPN' solubilized in organic solvents
    • Wangikar, P. P., Michels, P. C., Clark, D. S., Dordick, J. S. 1997. Structure and function of subtilisin BPN' solubilized in organic solvents. J. Am. Chem. Soc. 119: 70-76.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 70-76
    • Wangikar, P.P.1    Michels, P.C.2    Clark, D.S.3    Dordick, J.S.4
  • 33
    • 0024287893 scopus 로고
    • The effect of water on enzyme action in organic media
    • Zaks, A., Klibanov, A. 1988. The effect of water on enzyme action in organic media. J. Biol. Chem. 263: 8017-8021.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8017-8021
    • Zaks, A.1    Klibanov, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.