메뉴 건너뛰기




Volumn 20, Issue 2, 1997, Pages 93-101

Effect of the immobilization support on the hydrolytic activity of a cutinase from Fusarium solani pisi

Author keywords

Accurel PA6; Cutinase; Enzyme selectivity; Hydrolysis; Immobilization; NaY zeolite; Organic solvents; Thermal stability; Water content

Indexed keywords

CATALYSIS; CATALYST SELECTIVITY; COMPOSITION EFFECTS; ENZYME KINETICS; HYDROLYSIS; IONIC STRENGTH; ORGANIC SOLVENTS; PH; SODIUM COMPOUNDS; THERMODYNAMIC STABILITY; WATER; ZEOLITES;

EID: 0031081636     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00089-0     Document Type: Article
Times cited : (50)

References (31)
  • 1
    • 0016682066 scopus 로고
    • Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. Pisi
    • 1. Purdy, R. E. and Kolattukudy, P. E. Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry 1975, 14, 2824-2831
    • (1975) Biochemistry , vol.14 , pp. 2824-2831
    • Purdy, R.E.1    Kolattukudy, P.E.2
  • 2
    • 0001567583 scopus 로고
    • Cloning, expression, and characterization of cutinase, a fungal lipolytic enzyme
    • (Alberghina, L., Schmid, R. D., Verger, R., Eds.). VCH, New York
    • 2. Lauwereys, M., De Geus, P., De Meutter, J., Stanssens, P., and Matthyssens, G. Cloning, expression, and characterization of cutinase, a fungal lipolytic enzyme. In: Lipases: Structure, Mechanism and Genetic Engineering (Alberghina, L., Schmid, R. D., Verger, R., Eds.). VCH, New York, 1990, 243-251
    • (1990) Lipases: Structure, Mechanism and Genetic Engineering , pp. 243-251
    • Lauwereys, M.1    De Geus, P.2    De Meutter, J.3    Stanssens, P.4    Matthyssens, G.5
  • 4
    • 0029065498 scopus 로고
    • Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity
    • 4. Mannesse, M. L. M., Cox, R. C., Koops, B. C., Verheij, H. M., Hass, G. H., Egmond, M. R., Hijden, H. T. W. M., and Vlieg, J. Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity. Biochemistry 1995, 34, 6400-6407
    • (1995) Biochemistry , vol.34 , pp. 6400-6407
    • Mannesse, M.L.M.1    Cox, R.C.2    Koops, B.C.3    Verheij, H.M.4    Hass, G.H.5    Egmond, M.R.6    Hijden, H.T.W.M.7    Vlieg, J.8
  • 5
    • 0029205576 scopus 로고
    • Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles
    • 5. Melo, E. P., Aires-Barros, M. R., and Cabral, J. M. S. Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles. Appl. Biochem. Biotechnol. 1995, 50, 45-56
    • (1995) Appl. Biochem. Biotechnol. , vol.50 , pp. 45-56
    • Melo, E.P.1    Aires-Barros, M.R.2    Cabral, J.M.S.3
  • 6
    • 0000006162 scopus 로고
    • Ester synthesis by a recombinant cutinase in reversed micelles of a natural phospholipid
    • 6. Pinto-Sousa, A. M. C., Cabral, J. M. S., and Aires-Barros, M. R. Ester synthesis by a recombinant cutinase in reversed micelles of a natural phospholipid. Biocatalysis 1994, 9, 169-179
    • (1994) Biocatalysis , vol.9 , pp. 169-179
    • Pinto-Sousa, A.M.C.1    Cabral, J.M.S.2    Aires-Barros, M.R.3
  • 7
    • 0026501928 scopus 로고
    • Alginate as immobilization matrix and stabilizing agent in a two-phase liquid system: Application in lipase-catalysed reactions
    • 7. Hertzberg, S., Kvittingen, L., Anthonsen, T., and SkjaK-Broek, G. Alginate as immobilization matrix and stabilizing agent in a two-phase liquid system: Application in lipase-catalysed reactions. Enzyme Microb. Technol. 1992, 14, 42-47
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 42-47
    • Hertzberg, S.1    Kvittingen, L.2    Anthonsen, T.3    SkjaK-Broek, G.4
  • 8
    • 0025354941 scopus 로고
    • Lipolytic activities of a lipase immobilized on six selected supporting materials
    • 8. Shaw, J.-F., Chang, R.-C., Wang, F. F., and Wang, Y. J. Lipolytic activities of a lipase immobilized on six selected supporting materials. Biotechnol. Bioeng. 1990, 35, 132-137
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 132-137
    • Shaw, J.-F.1    Chang, R.-C.2    Wang, F.F.3    Wang, Y.J.4
  • 9
    • 0025331247 scopus 로고
    • Factors influencing the activity and thermostability of immobilized porcine pancreatic lipase
    • 9. Kery, V., Haplova, J., and Tihlárik, K. Factors influencing the activity and thermostability of immobilized porcine pancreatic lipase. J. Chem. Tech. Biotechnol. 1990, 48, 201-207
    • (1990) J. Chem. Tech. Biotechnol. , vol.48 , pp. 201-207
    • Kery, V.1    Haplova, J.2    Tihlárik, K.3
  • 10
    • 0025982410 scopus 로고
    • Immobilized enzymes in organic solvents
    • (Taylor, R. F., Ed.). Marcel Dekker, New York
    • 10. Tanaka, A. and Kawamoto, T. Immobilized enzymes in organic solvents. In: Protein Immobilization (Taylor, R. F., Ed.). Marcel Dekker, New York, 1991, 183-208
    • (1991) Protein Immobilization , pp. 183-208
    • Tanaka, A.1    Kawamoto, T.2
  • 11
    • 0025870959 scopus 로고
    • On the importance of the support material for enzymatic synthesis in organic media - Support effects at controlled water activity
    • 11. Adlercreutz, P. On the importance of the support material for enzymatic synthesis in organic media - support effects at controlled water activity. Eur. J. Biochem. 1991, 199, 609-614
    • (1991) Eur. J. Biochem. , vol.199 , pp. 609-614
    • Adlercreutz, P.1
  • 14
    • 0016979036 scopus 로고
    • Rapid colorimetric determination of free fatty acids
    • 14. Lowry, R. R. and Tinsley, I. J. Rapid colorimetric determination of free fatty acids. J. Am. Oil Chem. Soc. 1976, 53, 470-472
    • (1976) J. Am. Oil Chem. Soc. , vol.53 , pp. 470-472
    • Lowry, R.R.1    Tinsley, I.J.2
  • 16
    • 0024287153 scopus 로고
    • On the importance of the support material for bioorganic synthesis. Influence of water partition between solvent, enzyme, and solid support in water-poor reaction media
    • 16. Reslow, M., Adlercreutz, P., and Mattiasson, B. On the importance of the support material for bioorganic synthesis. Influence of water partition between solvent, enzyme, and solid support in water-poor reaction media. Eur. J. Biochem. 1988, 172, 573-578
    • (1988) Eur. J. Biochem. , vol.172 , pp. 573-578
    • Reslow, M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 19
    • 0026063822 scopus 로고
    • Hydrolysis and esterification with immobilized lipase on hydrophobic and hydrophilic zeolites
    • 19. Lie, E. and Molin, E. Hydrolysis and esterification with immobilized lipase on hydrophobic and hydrophilic zeolites. J. Chem. Tech. Biotechnol. 1991, 50, 549-553
    • (1991) J. Chem. Tech. Biotechnol. , vol.50 , pp. 549-553
    • Lie, E.1    Molin, E.2
  • 20
    • 0029636230 scopus 로고
    • Effects of sorbitol addition on the action of free and immobilized hydrolytic enzymes in organic media
    • 20. Triantafyllou, A. O., Wehtje, E., Adlercreutz, P., and Mattiasson, B. Effects of sorbitol addition on the action of free and immobilized hydrolytic enzymes in organic media. Biotechnol. Bioeng. 1995, 45, 406-414
    • (1995) Biotechnol. Bioeng. , vol.45 , pp. 406-414
    • Triantafyllou, A.O.1    Wehtje, E.2    Adlercreutz, P.3    Mattiasson, B.4
  • 21
    • 0023385987 scopus 로고
    • Rules for optimization of biocatalysis in organic solvents
    • 21. Laane, C., Boeren, S., Vos, K., and Veeger, C. Rules for optimization of biocatalysis in organic solvents. Biotechnol. Bioeng. 1987, 30, 81-87
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vos, K.3    Veeger, C.4
  • 22
    • 0028166667 scopus 로고
    • Partition coefficients of substrates and products and solvent selection for biocatalysis under nearly anhydrous conditions
    • 22. Yang, Z. and Robb, D. A. Partition coefficients of substrates and products and solvent selection for biocatalysis under nearly anhydrous conditions. Biotechnol. Bioeng. 1994, 43, 365-370
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 365-370
    • Yang, Z.1    Robb, D.A.2
  • 23
    • 0026190786 scopus 로고
    • Hydrolytic reactions in two-phase systems. Effect of water-immiscible organic solvents on stability and activity of acid phosphatase, β-glucosidase, and β-fructofuranosidase
    • 23. Cantarella, M., Cantarella, L., and Alfani, F. Hydrolytic reactions in two-phase systems. Effect of water-immiscible organic solvents on stability and activity of acid phosphatase, β-glucosidase, and β-fructofuranosidase. Enzyme Microb. Technol. 1991, 13, 547-553
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 547-553
    • Cantarella, M.1    Cantarella, L.2    Alfani, F.3
  • 24
    • 0025405410 scopus 로고
    • Solvent selection for biocatalysis in mainly organic systems: Predictions of effects on equilibrium position
    • 24. Halling, P. J. Solvent selection for biocatalysis in mainly organic systems: Predictions of effects on equilibrium position. Biotechnol. Bioeng. 1990, 35, 691-701
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 691-701
    • Halling, P.J.1
  • 25
    • 0028855057 scopus 로고
    • Role of solvents in the control of enzyme selectivity in organic media
    • 25. Carrea, G., Ottolina, G., and Riva, S. Role of solvents in the control of enzyme selectivity in organic media. Tibtech 1995, 13, 63-70
    • (1995) Tibtech , vol.13 , pp. 63-70
    • Carrea, G.1    Ottolina, G.2    Riva, S.3
  • 26
    • 0011439158 scopus 로고
    • Reaction kinetics of immobilized α-chymotrypsin in organic media. 1. Influence of solvent polarity. 2. Effects of substrate partition
    • 26. Wehtje, E., Adlercreutz, P., and Mattiasson, B. Reaction kinetics of immobilized α-chymotrypsin in organic media. 1. Influence of solvent polarity. 2. Effects of substrate partition. Biocatalysis 1993, 7, 149-176
    • (1993) Biocatalysis , vol.7 , pp. 149-176
    • Wehtje, E.1    Adlercreutz, P.2    Mattiasson, B.3
  • 27
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in non-conventional media: Theory, tests, and recommendations for experimental design and analysis
    • 27. Halling, P. J. Thermodynamic predictions for biocatalysis in non-conventional media: Theory, tests, and recommendations for experimental design and analysis. Enzyme Microb. Technol. 1994, 16, 178-206
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 178-206
    • Halling, P.J.1
  • 29
    • 0020751468 scopus 로고
    • Ionic strength: A neglected variable in enzyme technology
    • 29. Dale, B. E. and White, D. H. Ionic strength: A neglected variable in enzyme technology. Enzyme Microb. Technol. 1983, 5, 227-229
    • (1983) Enzyme Microb. Technol. , vol.5 , pp. 227-229
    • Dale, B.E.1    White, D.H.2
  • 30
    • 0027627398 scopus 로고
    • Synthesis of fatty acid esters by a recombinant cutinase in reversed micelles
    • 30. Sebastião, M. J., Cabral, J. M. S., and Aires-Barros, M. R. Synthesis of fatty acid esters by a recombinant cutinase in reversed micelles. Biotechnol. Bioeng. 1993, 42, 326-332
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 326-332
    • Sebastião, M.J.1    Cabral, J.M.S.2    Aires-Barros, M.R.3
  • 31
    • 0022013872 scopus 로고
    • Categorization of enzyme deactivations using a series-type mechanism
    • 31. Henley, J. P. and Sadana, A. Categorization of enzyme deactivations using a series-type mechanism. Enzyme Microb. Technol. 1985, 7, 50-60
    • (1985) Enzyme Microb. Technol. , vol.7 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.