메뉴 건너뛰기




Volumn 19, Issue 8, 1996, Pages 601-605

Comparative study of methodologies for obtaining β-glucosidase immobilized on dextran-modified silica

Author keywords

glucosidase; Dextran dialdehyde; Enzyme immobilization; Silica

Indexed keywords

ALDEHYDES; HEAT RESISTANCE; MOLECULAR STRUCTURE; SILICA; THERMODYNAMIC STABILITY;

EID: 0030445237     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00067-1     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 0027278213 scopus 로고
    • Biocatalysis and immobilized enzyme/cell bioreactors
    • 1. Abdul Mazid, M. Biocatalysis and immobilized enzyme/cell bioreactors. Biotechnology 1993, 11, 690-695
    • (1993) Biotechnology , vol.11 , pp. 690-695
    • Abdul Mazid, M.1
  • 2
    • 0023813410 scopus 로고
    • Medical applications of immobilized proteins, enzymes, and cells
    • (Wood, W. A. and Kellog, S. T., Eds.). Academic Press, San Diego
    • 2. Chang, T. M. S. Medical applications of immobilized proteins, enzymes, and cells. In: Methods in Enzymology Vol. 137 (Wood, W. A. and Kellog, S. T., Eds.). Academic Press, San Diego, 1988, 443-457
    • (1988) Methods in Enzymology , vol.137 , pp. 443-457
    • Chang, T.M.S.1
  • 6
    • 0018408815 scopus 로고
    • Enzyme stabilization by immobilization
    • 6. Klibanov, A. M. Enzyme stabilization by immobilization. Anal. Biochem. 1978, 93, 1-25
    • (1978) Anal. Biochem. , vol.93 , pp. 1-25
    • Klibanov, A.M.1
  • 7
    • 0025405523 scopus 로고
    • Multipoint attachment to a support protects enzyme from inactivation by organic solvents: α-Chymotrypsin in aqueous solutions of alcohols and diols
    • 7. Mozhaev, V. V., Segeeva, M. V., Belova, A. B., and Khmelnitsky, Y. L. Multipoint attachment to a support protects enzyme from inactivation by organic solvents: α-Chymotrypsin in aqueous solutions of alcohols and diols. Biotechnol. Bioeng. 1990, 35, 653-659
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 653-659
    • Mozhaev, V.V.1    Segeeva, M.V.2    Belova, A.B.3    Khmelnitsky, Y.L.4
  • 8
    • 0026955799 scopus 로고
    • Chemical crosslinking and stabilization of proteins and enzymes
    • 8. Wong, S. S. and Wong. L. J. C. Chemical crosslinking and stabilization of proteins and enzymes. Enzyme Microb. Technol. 1993, 14, 866-874
    • (1993) Enzyme Microb. Technol. , vol.14 , pp. 866-874
    • Wong, S.S.1    Wong, L.J.C.2
  • 9
    • 0021512923 scopus 로고
    • Peptide synthesis in aqueous-organic solvent mixtures with α-chymotrypsin immobilized to tresyl chloride-activated agarose
    • 9. Nilson, K. and Mosbach, K. Peptide synthesis in aqueous-organic solvent mixtures with α-chymotrypsin immobilized to tresyl chloride-activated agarose. Biotechnol. Bioeng. 1984, 26, 1146-1154
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 1146-1154
    • Nilson, K.1    Mosbach, K.2
  • 10
    • 0024029957 scopus 로고
    • Aldehyde-agarose gels as activated supports for the immobilization-stabilization of enzymes
    • 10. Guisan, J. M. Aldehyde-agarose gels as activated supports for the immobilization-stabilization of enzymes. Enzyme Microb. Technol. 1988, 10, 375-382
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 375-382
    • Guisan, J.M.1
  • 11
    • 0024675074 scopus 로고
    • Immobilization-stabilization of enzymes; variables that control the intensity of trypsin (amine)-agarose (aldehyde) multipoint attachment
    • 11. Blanco, R. M., Calvete, J. J., and Guisan, J. M. Immobilization-stabilization of enzymes; variables that control the intensity of trypsin (amine)-agarose (aldehyde) multipoint attachment. Enzyme Microb. Technol. 1989, 11, 353-358
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 353-358
    • Blanco, R.M.1    Calvete, J.J.2    Guisan, J.M.3
  • 12
    • 0024677047 scopus 로고
    • Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives
    • 12. Blanco, R. M. and Guisan, J. M. Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives. Enzyme Microb. Technol. 1989, 11, 360-366
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 360-366
    • Blanco, R.M.1    Guisan, J.M.2
  • 13
    • 0026417558 scopus 로고
    • Immobilization-stabilization of α-chymotrypsin by covalent attachment to aldehyde-agarose gels
    • 13. Guisan, J. M., Bastida, A., Cuesta, C., Fernandez-Lafuente, R., and Rosell, C. M. Immobilization-stabilization of α-chymotrypsin by covalent attachment to aldehyde-agarose gels. Biotechnol. Bioeng. 1991, 38, 1144-1152
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 1144-1152
    • Guisan, J.M.1    Bastida, A.2    Cuesta, C.3    Fernandez-Lafuente, R.4    Rosell, C.M.5
  • 14
    • 0027909727 scopus 로고
    • Stabilization of heteromeric enzyme by multipoint covalent immobilization: Penicillin G acylase from Kluyvera citrophila
    • 14. Guisan, J. M., Alvaro, G., Fernandez-Lafuente, R., Rosell, C. M., and Garcia, J. L. Stabilization of heteromeric enzyme by multipoint covalent immobilization: Penicillin G acylase from Kluyvera citrophila. Biotechnol. Bioeng. 1993, 42, 455-464
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 455-464
    • Guisan, J.M.1    Alvaro, G.2    Fernandez-Lafuente, R.3    Rosell, C.M.4    Garcia, J.L.5
  • 15
    • 0011318035 scopus 로고
    • Surface modification of proteins
    • 15. Reiner, R. and Doring, H. Surface modification of proteins. Enzyme Eng. 1978, 4, 111-116
    • (1978) Enzyme Eng. , vol.4 , pp. 111-116
    • Reiner, R.1    Doring, H.2
  • 16
    • 0021526166 scopus 로고
    • Thermal stabilization of amylolytic enzymes by covalent coupling to soluble polysaccharides
    • 16. Lenders, J. P. and Crichton, R. R. Thermal stabilization of amylolytic enzymes by covalent coupling to soluble polysaccharides. Biotechnol. Bioeng. 1984, 26, 1343-1351
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 1343-1351
    • Lenders, J.P.1    Crichton, R.R.2
  • 17
    • 0024278864 scopus 로고
    • Thermal stabilization of a chemically oriented modified pullulanase
    • 17. Germain, P., Maskaren, J. S., and Crichton, R. R. Thermal stabilization of a chemically oriented modified pullulanase. Biotechnol. Bioeng. 1988, 32, 249-254
    • (1988) Biotechnol. Bioeng. , vol.32 , pp. 249-254
    • Germain, P.1    Maskaren, J.S.2    Crichton, R.R.3
  • 18
    • 84996075885 scopus 로고
    • Relation between stabilization and rigidification of the three-dimensional structure of an enzyme
    • 18. Germain, P., Slagmolen, T., and Crichton, R. R. Relation between stabilization and rigidification of the three-dimensional structure of an enzyme. Biotechnol. Bioeng. 1988, 33, 563-569
    • (1988) Biotechnol. Bioeng. , vol.33 , pp. 563-569
    • Germain, P.1    Slagmolen, T.2    Crichton, R.R.3
  • 19
    • 0026111220 scopus 로고
    • Studies on stabilization of amylase by covalent coupling to soluble polysaccharides
    • 19. Srivastava, R. A. K. Studies on stabilization of amylase by covalent coupling to soluble polysaccharides. Enzyme Microb. Technol. 1991, 13, 164-170
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 164-170
    • Srivastava, R.A.K.1
  • 20
    • 0028013436 scopus 로고
    • Functional changes of dextran-modified alkaline proteinase from alkalophilic Bacillus sp.
    • 20. Yamagata, Y., Arakawa, K., Yamaguchi, M., Kobayashi, M., and Ichishima, E. Functional changes of dextran-modified alkaline proteinase from alkalophilic Bacillus sp. Enzyme Microb. Technol. 1994, 16, 99-103
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 99-103
    • Yamagata, Y.1    Arakawa, K.2    Yamaguchi, M.3    Kobayashi, M.4    Ichishima, E.5
  • 21
    • 0022060787 scopus 로고
    • Immobilization of a soluble chemically thermostabilized enzyme
    • 21. Lenders, J. P., Germain, P., and Crichton, R. R. Immobilization of a soluble chemically thermostabilized enzyme. Biotechnol. Bioeng. 1985, 27, 572-578
    • (1985) Biotechnol. Bioeng. , vol.27 , pp. 572-578
    • Lenders, J.P.1    Germain, P.2    Crichton, R.R.3
  • 22
    • 0023929184 scopus 로고
    • Characterization of a chemically modified β-amylase immobilized on porous silica
    • 22. Germain, P. and Crichton, R. R. Characterization of a chemically modified β-amylase immobilized on porous silica. J. Chem. Technol. Biotechnol. 1988, 41, 297-315
    • (1988) J. Chem. Technol. Biotechnol. , vol.41 , pp. 297-315
    • Germain, P.1    Crichton, R.R.2
  • 24
    • 0024438580 scopus 로고
    • Development of effective cross-linking method for bioactive substance-enzyme immobilization using glutaraldehyde oligomers
    • 24. Nakagawa, I., Izawa, K., Yagi, S., Shibukawa, A., Tanaka H., Tashima, T., and Imai, M. Development of effective cross-linking method for bioactive substance-enzyme immobilization using glutaraldehyde oligomers. Chem. Pharm. Bull. 1989, 37, 2463-2466
    • (1989) Chem. Pharm. Bull. , vol.37 , pp. 2463-2466
    • Nakagawa, I.1    Izawa, K.2    Yagi, S.3    Shibukawa, A.4    Tanaka, H.5    Tashima, T.6    Imai, M.7
  • 25
    • 0011319339 scopus 로고
    • Polysaccharides as drug carriers
    • In: Control Release Technol
    • 25. Schacht, E. Vandoorne F., Verneersch, J., and Duncan, R., Polysaccharides as drug carriers. In: Control Release Technol, Acs. Symp. Sci., 1987, 348, 188-200
    • (1987) Acs. Symp. Sci. , vol.348 , pp. 188-200
    • Schacht, E.1    Vandoorne, F.2    Verneersch, J.3    Duncan, R.4
  • 26
    • 0018367097 scopus 로고
    • Detergents linked to polysaccharides: Preparations and effects on membranes and cells
    • 26. Pitha, J., Kociolek, K., and Caron, M. Detergents linked to polysaccharides: Preparations and effects on membranes and cells. Eur. J. Biochem. 1979, 94, 11-18
    • (1979) Eur. J. Biochem. , vol.94 , pp. 11-18
    • Pitha, J.1    Kociolek, K.2    Caron, M.3
  • 27
    • 84913282760 scopus 로고
    • Quantitative organic analysis
    • Longmans Green and Co., New York
    • 27. Vogel, A. I. Quantitative organic analysis. In: Elementary Practical Organic Chemistry. Longmans Green and Co., New York, 1958, 734-746
    • (1958) Elementary Practical Organic Chemistry , pp. 734-746
    • Vogel, A.I.1
  • 28
    • 4043071644 scopus 로고
    • The cyano-hydridoborate anion as a selective reducing agent
    • 28. Borch, R. F., Bernstein, M. D., and Dupont Durst, H. The cyano-hydridoborate anion as a selective reducing agent. J. Am. Chem. Soc. 1971, 93, 2897-2904
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 2897-2904
    • Borch, R.F.1    Bernstein, M.D.2    Dupont Durst, H.3
  • 29
    • 0017268663 scopus 로고
    • Kinetics of immobilized enzymes
    • 29. Goldstein, L. Kinetics of immobilized enzymes. Meth. Enzymol. 1976, 44, 397-450
    • (1976) Meth. Enzymol. , vol.44 , pp. 397-450
    • Goldstein, L.1
  • 30
    • 0010496123 scopus 로고
    • The physico-chemical properties of siliceous enzyme supports and their effects on composite performance
    • Ed. D. E. Leyden and W. Collins N.Y. Gordon and Breach
    • 30. Eaton, D. L. The physico-chemical properties of siliceous enzyme supports and their effects on composite performance. Ed. D. E. Leyden and W. Collins N.Y. In: Silylated Surfaces. Gordon and Breach, 1980, 201-211
    • (1980) Silylated Surfaces , pp. 201-211
    • Eaton, D.L.1
  • 31
    • 0026878360 scopus 로고
    • Additional stabilization of penicillin G acylase-agarose derivatives by controlled chemical modification with formaldehyde
    • 31. Fernandez-Lafuente, R., Rosell, C. M., Alvaro, G., and Guisan, J. M. Additional stabilization of penicillin G acylase-agarose derivatives by controlled chemical modification with formaldehyde. Enzyme Microb. Technol. 1992, 14, 489-495
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 489-495
    • Fernandez-Lafuente, R.1    Rosell, C.M.2    Alvaro, G.3    Guisan, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.