Functional stabilization of trypsin by conjugation with β-cyclodextrin-modified carboxymethylcellulose

Preparative Biochemistry and Biotechnology

Volumn 33, Issue 1, 2003, Pages 53-66

  Villalonga, María L ^a   Fernández, Michael ^a   Fragoso, Alex ^b   Cao, Roberto ^b   Villalonga, Reynaldo ^a  

^a UNIVERSITY OF MATANZAS   (Cuba)

^b UNIVERSITY OF HAVANA   (Cuba)

Author keywords

cyclodextrin; Carboxymethylcellulose; Enzyme stability; Modified enzyme; Trypsin

Indexed keywords

BETA-CYCLODEXTRINS; CARBOXYMETHYLCELLULOSE; CYCLODEXTRINS; ENZYME ACTIVATION; ENZYME STABILITY; ISOENZYMES; KINETICS; MACROMOLECULAR SUBSTANCES; PROTEIN BINDING; PROTEIN DENATURATION; TEMPERATURE; TRYPSIN;

BOS TAURUS; BOVINAE;

EID: 0037252492     PISSN: 10826068     EISSN: None     Source Type: Journal    
DOI: 10.1081/PB-120018369     Document Type: Article

References (24)

1. Sundaram, P.V.; Venkatesh, R. Retardation of thermal and urea induced inactivation of α-chymotrypsin by modification with carbohydrate polymers. Protein Engng. 1998, 11, 691-698.
2. Longo, M.A.; Combes, D. Influence of surface hydrophilic/hydrophobic balance on enzyme properties. J. Biotechnol. 1997, 58, 21-32.
3. Wang, Ch.; Eufemi, M.; Turano, C.; Giartosio, A. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 1996, 35, 7299-7307.
4. Srivastava, R.A.K. Studies on stabilization of amylase by covalent coupling to soluble polysaccharides. Enzyme Microb. Technol. 1991, 13, 164-170.
5. Darias, R.; Villalonga, R. Functional stabilization of cellulase by covalent modification with chitosan. J. Chem. Technol. Biotechnol. 2001, 76, 489-493.
6. Gómez, L.; Villalonga, R. Functional stabilization of invertase by covalent modification with pectin. Biotechnol. Lett. 2000, 22, 1191-1195.
7. Gómez, L.; Ramírez, H.L.; Villalonga, R. Stabilization of invertase by modification of sugar chains with chitosan. Biotechnol. Lett. 2000, 22, 347-350.
8. Fernández, M.; Fragoso, A.; Cao, R.; Baños, M.; Villalonga, M.L.; Villalonga, R. Stabilization of trypsin by chemical modification with β-cyclodextrin monoaldehyde. Biotechnol. Lett. 2002, 24, 1455-1459.
9. Szejtli, J. Introduction and general overview of cyclodextrins. Chem. Rev. 1998, 98, 1743-1754.
10. Szejtli, J.; Osa, T. Comprehensive Supramolecular Chemistry; Pergamon: Oxford, UK, 1996; Vol. 3, 5-40.
11. Schneider, H.J.; Xiao, F. Binding and catalysis with a metal-induced ternary complex of an ethylenediamine-substituted cyclodextrin. J. Chem. Soc. Perkin Trans. 1992, 2, 387-391.
12. Schwert, G.B.; Takenaka, Y. A spectrophotometric determination of trypsin and chymotrypsin. Biochim. Biophys. Acta 1955, 16, 570-575.
13. Laskowski, M. Trypsinogen and trypsin. Methods Enzymol. 1955, 2, 26-36.
14. Dubois, M.K.; Gilles, A.; Hamilton, J.K.; Rebers, P.A.; Smith, F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 1956, 28, 350-356.
15. Lowry, O.H.; Rosebrough, N.J.; Farr, A.L.; Randall, R. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193, 265-275.
16. Bruneel, D.; Schacht, E. Chemical modification of pullulan: 1. Periodate oxidation. Polymer 1993, 34, 2628-2632.
17. Kaneko, T.; Hamamoto, T.; Horikoshi, K. Molecular cloning and nucleotide sequence of the cyclomaltodextrin glucanotransferase gene from alkalophilic Bacillus sp. Strain No. 38-2. J. Gen. Microbiol 1988, 139, 97-105.
18. Martinek, K.; Klibanov, A.M.; Goldmacher, V.S.; Berezin, I.V. The principles of enzyme stabilization I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion. Biochim. Biophys. Acta. 1977, 485, 1-12.
19. Mozhaev, V.V.; Martinek, K. Inactivation and reactivation of proteins (enzymes). Enzyme Microb. Technol. 1982, 4, 299-309.
20. Gómez, L.; Ramírez, H.L.; Villalonga, R. Chemical modification of α-amylase by sodium alginate. Acta Biotechnol. 2001, 21, 265-273.
21. Perona, J.J.; Craik, C.S. Structural basis of substrate specificity in the serine proteases. Protein Sci. 1995, 4, 337-360.
22. Marshall, J.J. Manipulation of the properties of enzymes by covalent attachment of carbohydrate. Trends Biochem. Sci. 1978, 3, 79-81.
23. Moskvichyov, B.V.; Komarov, E.V.; Ivanova, G.P. Study of trypsin thermodenaturation process. Enzyme Microb. Technol. 1986, 8, 498-502.
24. Ericsson, B.; Hegg, P.O. Effects of amphiphiles on trypsin activity and conformation. J. Disper. Sci. Technol. 1987, 8, 289-301.