Preparation of a stable biocatalyst of bovine liver catalase using immobilization and postimmobilization techniques

Biotechnology Progress

Volumn 19, Issue 3, 2003, Pages 763-767

  Betancor, Lorena ^a   Hidalgo, Aurelio ^a   Fernández Lorente, Gloria ^a   Mateo, Cesar ^a   Fernández Lafuente, Roberto ^a   Guisan, José M ^a  

^a CSIC   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCATALYSTS; CATALYST ACTIVITY; CATALYST SUPPORTS; CROSSLINKING; DISSOCIATION; ENZYME IMMOBILIZATION; ENZYME KINETICS;

DILUTION;

BIOTECHNOLOGY;

BOS TAURUS; BOVINAE;

EID: 0038796679     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp025785m     Document Type: Article

References (26)

1. Zámocky, M.; Koller, F. Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis. Prog. Biophys. Mol. Biol. 1999, 72, 19-66.
2. Costa, S.; Tzanko, T.; Paar, A.; Gudelj, M.; Gübitz, G. M.; Cavaco-Paulo, A. Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents. Enzyme Microb. Technol. 2001, 28, 815-819.
3. 2. Appl. Biochem. Biotechnol. 1995, 50, 291-303.
4. Tarhan, L. Enzymatic properties of immobilized catalase on protein coated supports. Biomed. Biochim. Acta 1990, 49, 5, 307-316.
5. Fernández-Lafuente, R.; Rodriguez, V.; Guisán, J. M. The coimmobilization of D-amino acid oxidase and catalase enables the quantitative transformatin of D-amino acids (D-phenylalanine) into α-keto acids (phenylpyruvic acid). Enzyme Microb. Technol. 1998, 23, 28-33.
6. Blandino, A.; Macías, M.; Cantero, D. Modelling and simulation of a bienzymatic reaction system co-immobilized within hydrogel-membrane liquid-core capsules. Enzyme Microb. Technol. 2002, 31, 556-565.
7. Schoevaart, R.; Kieboom, T. Combined catalytic reactions-Nature's way. Chem Innov. 2001, 33-38.
8. Percy, M., E. Catalase: an old enzyme with a new role? Can. J. Biochem. Cell. Biol. 1984, 62, 1006-1014.
9. Solas, M. T.; Vicente, C.; Xavier, L.; Legaz, M. E. Ionic adsorption of catalase on bioskin: kinetic and ultrastructural studies. J. Biotechnol. 1994, 33, 63-70.
10. Yabe, Y.; Nishikawa, M.; Tamada, A.; Takakura, Y.; Hashida, M. Targeted delivery and improved therapeutic potential of catalase by chemical modification: combination with superoxide dismutase derivatives. J. Pharmacol. Exp. Ther. 1999, 289(2), 1176-1184.
11. 2+-chelating membrane affinity chromatography for purification of bovine liver catalase. Biomed. Chromatogr. 1999, 13, 229-234.
12. Ghadermarzi, M.; Moosavi-Movahedi, A.; Ghadermarzi, M. Influence of different types of effectors on the kinetic parameters of suicide inactivation of catalase by hydrogen peroxide. Biochim. Biophys. Acta 1999, 1431, 30-36.
13. Poltorak, O. M.; Chukhary, E. S.; Torshin, I. Y. Dissociative thermal inactivation, stability and activity of oligomeric enzymes. Biochemistry (Moscow) 1998, 63, 360-369.
14. Attwood, P. V.; Geeves, M. A. Changes in catalytic activity and association state of pyruvate carboxylase wich are dependent on enzyme concentration. Arch. Biochem. Biophys. 2002, 401, 63-72.
15. Mozahev, V. V.; Klibanov, A. M.; Goldmacher, V. S.; Berezin, I. V. Operational stability of copolimerized enzymes at elevated temperatures. Biotechnol. Bioeng. 1990, 25, 1937-1945.
16. Poltorak, O. M.; Chukhray, E. S.; Torshin, I. Y.; Atyaksheva, L. F.; Trevom, M. D.; Chaplin, M. F. Catalytic properties, stability and the structure of the conformational lock in the alkaline phosphatase from Escherichia coli. J. Mol. Catal. B: Enzym. 1999, 7, 165-172.
17. Fernández-Lafuente, R.; Rodriguez, V.; Mateo, C.; Penzol, G.; Hernández-Justiz O.; Irazoqui, G.; Villarino, A.; Ovsejevi, K.; Batista, F.; Guisán, J. M. Stabilization of multimeric enzymes via immobilization and post-immobilization techniques. J. Mol. Catal. B: Enzym. 1999, 7, 181-189.
18. Balcao, V. M.; Mateo, C.; Fernández-Lafuente, R.; Malcata, F. X.; Guisan, J. M. Structural and functional stabilization of L-asparaginase via multisubunit immobilization onto highly activated supports. Biotechnol. Prog. 2001, 17(3), 537-542.
19. Fernández-Lafuente, R.; Hernández-Ruiz, O.; Mateo, C.; Terreni, M.; Alonso, J.; García-López, J.; Moreno, M. A.; Guisan, J. M. Stabilization of a tetrameric enzyme (α-amino acid ester hydrolase from Acetobacter turbidans, enables a very improved performance of ampicillin synthesis. J. Mol. Catal B: Enzymol. 2001, 11, 633-638.
20. Guisán, J. M. Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes. Enzyme Microb. Technol. 1988, 10, 375-382.
21. Guisan, J. M.; Rodriguez, V.; Rosell, C. M.; Soler, G.; Bastida, A.; Blanco, R. M.; Fernández-Lafuente, R.; García Junceda, E. Stabilization of immobilized enzymes by chemical modification with polyfunctional macromolecules. In Immobilization of Enzymes and Cells; Methods in Biotechnology 1; Bickerstaff, G., Ed.; The Humana Press: Totowa, NJ, 1997; pp 289-298.
22. Aebi, H. E. Catalase. In Methods of Enzymatic Analysis, 3rd ed.; Bergmeyer, H. U., Ed.; Verlag Chemie: Weinheim, Germany, 1974; pp 672-684.
23. Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing theprinciple of protein-dye binding. Anal. Biochem. 1976, 72, 248-254
24. Bastida, A.; Sabuquillo, P.; Armisen, P.; Fernández-Lafuente, R.; Huguet, J.; Guisan, J. M. A single sep purification, immobilization and hyperactivation of lipases via interfacial adsorption on stronlgy hidrophobic support. Biotechnol. Bioeng. 1998, 58, 486-493.
25. Blanco, R. M.; Calvete, J. J.; Guisan, J. M. Immobilization-stabilization of enzymes variables that control the intensity of the trypsin (amine)-agarose (aldehyde) multipointy attachment. Enzyme Microb. Technol. 1989, 11, 353-359.
26. Guisán, J. M.; Bastida, A.; Blanco, R. M.; Fernández-Lafuente, R.; García-Junceda, E. Immobilization of enzymes by chemical modification with polyfunctional macromolecules. In Immobilization of Enzymes and Cells; Methods in Biotechnology 1; Bickerstaff, G., Ed.; The Humana Press: Totowa, NJ, 1997; pp 261-275.