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Volumn 25, Issue 5, 2007, Pages 373-381

Chemical thiolation strategy: A determining factor in the in the properties of thiol-bound biocatalysts

Author keywords

Galactosidase; Enzyme immobilization; Organic co solvents; Stabilization; Thiolsuphinate

Indexed keywords

DERIVATIVES; DESORPTION; ENZYME IMMOBILIZATION; FUNCTIONAL GROUPS; ORGANIC SOLVENTS;

EID: 35148816633     PISSN: 10242422     EISSN: 10292446     Source Type: Journal    
DOI: 10.1080/10242420701510460     Document Type: Article
Times cited : (7)

References (24)
  • 1
    • 0002951978 scopus 로고
    • Solid-phase thiolsulphinates for the reversible immobilization of thiols
    • Batista-Viera, F., Manta, C. and Carlsson, J. (1994) Solid-phase thiolsulphinates for the reversible immobilization of thiols. Appl Biochem Biotechnol, 44, pp. 1-14.
    • (1994) Appl Biochem Biotechnol , vol.44 , pp. 1-14
    • Batista-Viera, F.1    Manta, C.2    Carlsson, J.3
  • 3
    • 0037413434 scopus 로고    scopus 로고
    • Effect of increasing co-solvent concentration on the stability of soluble and immobilized β-galactosidase
    • Brena, BM, Irazoqui, G., Giacomini, C. and Batista-Viera, F. (2003) Effect of increasing co-solvent concentration on the stability of soluble and immobilized β-galactosidase. J Mol Cat B: Enzym, 21, pp. 25-29.
    • (2003) J Mol Cat B: Enzym , vol.21 , pp. 25-29
    • Brena, B.M.1    Irazoqui, G.2    Giacomini, C.3    Batista-Viera, F.4
  • 5
    • 0018115212 scopus 로고
    • Protein thiolation and reversible protein-protein conjugation
    • Carlsson, J., Drevin, H. and Axén, R. (1978) Protein thiolation and reversible protein-protein conjugation. Biochem J, 173, pp. 723-737.
    • (1978) Biochem J , vol.173 , pp. 723-737
    • Carlsson, J.1    Drevin, H.2    Axén, R.3
  • 9
    • 0032479881 scopus 로고    scopus 로고
    • Immobilization of β-galactosidase from Kluyveromyces lactis on silica and agarose: Comparison of different methods
    • Giacomini, C., Villarino, A., Franco-Fraguas, L. and Batista-Viera, F. (1998) Immobilization of β-galactosidase from Kluyveromyces lactis on silica and agarose: Comparison of different methods. J Mol Cat B: Enzym, 4, pp. 313-327.
    • (1998) J Mol Cat B: Enzym , vol.4 , pp. 313-327
    • Giacomini, C.1    Villarino, A.2    Franco-Fraguas, L.3    Batista-Viera, F.4
  • 10
    • 0035931373 scopus 로고    scopus 로고
    • Influence of the immobilization chemistry on the properties of immobilized β-galactosidase
    • Giacomini, C., Irazoqui, G., Batista-Viera, F. and Brena, BM (2001) Influence of the immobilization chemistry on the properties of immobilized β-galactosidase. J Mol Cat B: Enzym, 11, pp. 597-606.
    • (2001) J Mol Cat B: Enzym , vol.11 , pp. 597-606
    • Giacomini, C.1    Irazoqui, G.2    Batista-Viera, F.3    Brena, B.M.4
  • 11
    • 0021471834 scopus 로고
    • A mathematical analysis of enzyme stabilization by a series-type mechanism: Influence of chemical modifiers
    • Henley, JP and Sadana, A. (1984) A mathematical analysis of enzyme stabilization by a series-type mechanism: Influence of chemical modifiers. Biotechnol Bioeng, 26, pp. 959-969.
    • (1984) Biotechnol Bioeng , vol.26 , pp. 959-969
    • Henley, J.P.1    Sadana, A.2
  • 13
    • 0037083052 scopus 로고    scopus 로고
    • Generating favorable nano-enviroments for thermal and solvent stabilization of immobilized β-galactosidases
    • Irazoqui, G., Villarino, A., Batista-Viera, F. and Brena, BM (2002) Generating favorable nano-enviroments for thermal and solvent stabilization of immobilized β-galactosidases. Biotechnol Bioeng, 77:4, pp. 430-434.
    • (2002) Biotechnol Bioeng , vol.77 , Issue.4 , pp. 430-434
    • Irazoqui, G.1    Villarino, A.2    Batista-Viera, F.3    Brena, B.M.4
  • 14
    • 0020999167 scopus 로고
    • Stabilization of enzymes against thermal inactivation
    • Klibanov, AM (1983) Stabilization of enzymes against thermal inactivation. Adv Appl Microbiol, 29, pp. 1-28.
    • (1983) Adv Appl Microbiol , vol.29 , pp. 1-28
    • Klibanov, A.M.1
  • 15
    • 0034111128 scopus 로고    scopus 로고
    • Influence in conformational stability of enzymes immobilized on epoxy-activated supports by favouring additional multipoint covalent attachment
    • Mateo, C., Abian, O., Fernandez-Lafuente, R. and Guisán, JM (2000) Influence in conformational stability of enzymes immobilized on epoxy-activated supports by favouring additional multipoint covalent attachment. Enzyme Microb Technol, 26, pp. 509-515.
    • (2000) Enzyme Microb Technol , vol.26 , pp. 509-515
    • Mateo, C.1    Abian, O.2    Fernandez-Lafuente, R.3    Guisán, J.M.4
  • 17
    • 35148838038 scopus 로고    scopus 로고
    • NCBI (National Center for Biotechnology Information)
    • NCBI (National Center for Biotechnology Information)
  • 19
    • 0031936730 scopus 로고    scopus 로고
    • β-Galactosidase from Kluyveromices lactis immobilized on to thiolsulphinate/thiolsulfonate supports for lactose hydrolysis in milk and dairy by-products
    • Ovsejevi, K., Grazú, V. and Batista-Viera, F. (1998) β-Galactosidase from Kluyveromices lactis immobilized on to thiolsulphinate/thiolsulfonate supports for lactose hydrolysis in milk and dairy by-products. Biotechnol Tech, 12:2, pp. 143-148.
    • (1998) Biotechnol Tech , vol.12 , Issue.2 , pp. 143-148
    • Ovsejevi, K.1    Grazú, V.2    Batista-Viera, F.3
  • 20
    • 35148822233 scopus 로고
    • Comparison of various methods to determine kinetic constants for β-galactosidase in soluble and immobilised states
    • Peter, J., Prenosil, JE and Bourne, JR (1994) Comparison of various methods to determine kinetic constants for β-galactosidase in soluble and immobilised states. J Chem Tech Biotechnol, 8:4, pp. 705-709.
    • (1994) J Chem Tech Biotechnol , vol.8 , Issue.4 , pp. 705-709
    • Peter, J.1    Prenosil, J.E.2    Bourne, J.R.3
  • 21
    • 0023435073 scopus 로고
    • Single-step unimolecular non-first-order enzyme deactivation kinetics
    • Sadana, A. and Henley, JP (1987) Single-step unimolecular non-first-order enzyme deactivation kinetics. Biotechnol Bioeng, 30, pp. 717-723.
    • (1987) Biotechnol Bioeng , vol.30 , pp. 717-723
    • Sadana, A.1    Henley, J.P.2
  • 23
    • 0032839573 scopus 로고    scopus 로고
    • The concept of the unfolding region for approaching the mechanism of enzyme stabilization
    • Ulbrich-Hoffman, R., Arnold, U. and Mansfeld, J. (1999) The concept of the unfolding region for approaching the mechanism of enzyme stabilization. J Mol Cat B: Enzym, 7, pp. 125-131.
    • (1999) J Mol Cat B: Enzym , vol.7 , pp. 125-131
    • Ulbrich-Hoffman, R.1    Arnold, U.2    Mansfeld, J.3
  • 24
    • 0001722763 scopus 로고
    • β-Galactosidase
    • Academic Press, New York
    • Wallenfelds, K. and Weil, R. (1972) β-Galactosidase. The enzymes. 7, pp. 17-663. Academic Press, New York
    • (1972) The Enzymes , vol.7 , pp. 17-663
    • Wallenfelds, K.1    Weil, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.