Immobilised enzymes: Carrier-bound or carrier-free?

Current Opinion in Biotechnology

Volumn 14, Issue 4, 2003, Pages 387-394

  Cao, Linqiu ^a   van Langen, Luuk ^b   Sheldon, Roger A ^a,b  

^a DELFT UNIVERSITY OF TECHNOLOGY   (Netherlands)

^b CLEA Technologies   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; ENZYME;

BIOTRANSFORMATION; CROSS LINKING; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SUBSTRATE; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; REVIEW; THERMOSTABILITY;

EID: 0041430560     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(03)00096-X     Document Type: Review

References (46)

1. Mosbach K: Immobilised enzymes and cells (Part B). Methods Enzymol 1987, Vol. 135.
2. Hartmeier W: Immobilised Biocatalysts. Berlin: Springer-Verlag, 1988.
3. Clark D.S. Can immobilisation be exploited to modify enzyme activity? Trends Biotechnol. 12:1994;439-443.
4. Cabral JMS, Kennedy JF: Immobilisation techniques for altering thermal stability of enzymes. In Thermostability of Enzymes. Edited by Gupta MN. Berlin: Springer Verlag; 1993:163-179.
5. Rocchietti S., Urrutia A.S.V., Pregnolato M., Tagliani A., Guisan J.M., Fernandez-Lafuente R., Terreni M. Influence of the enzyme derivative preparation and substrate structure on the enantioselectivity of penicillin G acylase. Enzyme Microb Technol. 31:2002;88-93.
6. Tischer W., Kasche V. Immobilized enzymes: crystals or carriers? Trends Biotechnol. 17:1999;326-335.
7. Bryjak J., Kolarz B.N. Immobilisation of trypsin on acrylic copolymers process. Biochemistry. 33:1998;409-417.
8. Janssen M.H.A., van Langen L.M., Pereira S.R.M., van Rantwijk F., Sheldon R.A. Evaluation of the performance of immobilised penicillin G acylase using active-site titration. Biotechnol Bioeng. 78:2002;425-432.
9. Boller T., Meier C., Menzler S. Eupergit oxirane acrylic beads: how to make the enzyme fit for biocatalysts. Org Process Res Develop. 6:2002;509-519 Many interesting examples on the use of Eupergit carrier for enzyme immobilisation are provided.
10. Quiocho F.A., Richards F.M. Intermolecular cross-linking of a protein in the crystalline state: carboxypeptidase A. Proc Natl Acad Sci USA. 52:1964;833-839.
11. Alter G.M., Leussing D.L., Neurath H., Vallee B.L. Kinetic properties of carboxypeptidase B in solutions and crystals. Biochemistry. 16:1977;3663-3668.
12. St Clair N.L., Navia M.A. Cross-linked enzyme crystals as robust biocatalysts. J Am Chem Soc. 114:1992;7314-7316.
13. Habeeb A.F.S.A. Preparation of enzymically active, water-insoluble derivatives of trypsin. Arch Biochem Biophys. 119:1967;264-268.
14. Jansen E.F., Olson A.C. Properties and enzymatic activities of papain insolubilized with glutaraldehyde. Arch Biochem Biophys. 129:1969;221-228.
15. Cao L., van Rantwijk F., Sheldon R.A. Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase. Org Lett. 2:2000;1361-1364 It was demonstrated that, instead of the crystallization enzyme, aggregates can be used to prepare CLEAs with comparable or improved performance in comparison with CLECs.
16. Cheetham P.S.J. What makes a good biocatalyst? J Biotechnol. 66:1998;3-10.
17. Katchalski-Katzir E., Kraemer D.M. Eupergit C, a carrier for immobilization of enzymes of industrial potential. J Mol Catal B Enzym. 10:2000;157-176.
18. Messing RA: Immobilized Enzymes for Industrial Reactors. London: Academic Press; 1975.
19. Gemeiner P: Materials for enzyme engineering. In Enzyme Engineering - Immobilised Biosystems. England: Ellis Horwood Limited; 1992:13-119.
20. Van Roon J., Beeftink R., Schroen K., Tramper H. Assessment of intraparticle biocatalytic distribution as a tool in rational formulation. Curr Opin Biotechnol. 13:2002;398-405.
21. Amotz S: Method for production of an immobilized enzyme preparation by means of a crosslinking agent. (Novo Industri A/S) 1987; US 4,665,028.
22. Quiocho F.A., Richards F.M. The enzyme behaviors of carboxypeptidase-A in the solid state. Biochemistry. 5:1966;4062-4076.
23. Zarborsky O: Immobilised Enzymes. Cleveland: CRC Press; 1973.
24. Broun G., Selegny E., Avrameas S., Thomas D. Enzymatically active membranes: some properties of cellophane membranes supporting crosslinked enzymes. Biochim Biophys Acta. 185:1969;260-262.
25. Manecke G. Immobilization of enzymes by various synthetic polymers. Biotechnol Bioeng Symp. 3:1972;185-187.
26. Mosbach K. Enzymes bound to artificial matrixes. Sci Am. 224:1971;26-33.
27. Tüchsen E., Ottesen M. Kinetic properties of subtilisin type Carlsberg in the crystalline state. Carlsberg Res Commun. 42:1977;407-420.
28. Alter G.M., Leussing D.L., Neurath H., Vallee B.L. Kinetic properties of carboxypeptidase B in solutions and crystals. Biochemistry. 16:1977;3663-3668.
29. Lee K.M., Blaghen M., Samama J.P., Biellmann J.F. Cross-linked crystalline horse liver alcohol dehydrogenase as a redox catalyst: activity and stability towards organic solvent. Bioorg Chem. 14:1986;202-210.
30. St Clair N.L., Navia M.A. Cross-linked enzyme crystals as robust biocatalysts. J Am Chem Soc. 114:1992;7314-7316.
31. Lalonde J. Practical catalysis with enzyme crystals. Chemtech. 27:1997;38-45.
32. Margolin A.L. Novel crystalline catalysts. Trends Biotechnol. 14:1996;223-230.
33. Häring D., Schreier P. Cross-linked enzyme crystals. Curr Opin Chem Biol. 3:1999;35-38.
34. Rothstein F: Differential precipitation of proteins: science and technology. In Protein Purification Process Engineering, Edited by Harrison RG. New York: Marcel Dekker, Inc; 1994:115-208.
35. Cao L., van Langen L.M., van Rantwijk F., Sheldon R.A. Cross-linked aggregates of penicillin acylase: robust catalysts for the synthesis of β-lactam antibiotics. J Mol Catal B Enzym. 11:2001;665-670.
36. Tomimatsu Y., Jansen E.F., Gaffield W., Olson A.C. Physical chemical observations on the α-chymotrypsin glutaraldehyde system during formation of an insoluble derivative. J Colloid Interface Sci. 36:1971;51-64.
37. Lopez-Serrano P., Cao L., van Rantwijk F., Sheldon R.A. Cross-linked enzyme aggregates with enhanced activity: application to lipases. Biotechnol Lett. 24:2002;1379-1383.
38. Cao L, van Langen LM, Janssen MHA, Sheldon RA: Preparation and properties of cross-linked aggregates of penicillin acylase and other enzymes. Eur Pat Appl 1999; EP1088887A1.
39. Noritomi H., Koyama K., Kato S., Nagahama K. Increased thermostability of cross-linked enzyme crystals of subtilisin in organic solvents. Biotechnol Technol. 12:1998;467-469.
40. Visuri K., Pastrinen O., Wu X.Y., Maekinen K., Leisola M. Stability of native and crosslinked crystalline glucose isomerase. Biotechnol Bioeng. 64:1999;377-380.
41. Daryl K., Eggers A., Joan S. Valentine molecular confinement influences protein structure and enhances thermal protein stability. Protein Sci. 10:2001;250-261.
42. Mozhaev V.V., Sergeeva V., Belova A.B., Khmelnitski 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. 35:1990;653-659.
43. Huang D.B., Clint F., Ainsworth F.J.S., Marianne S. Three quaternary structures for a single protein. Proc Natl Acad Sci USA. 93:1996;7012-7017.
44. Cao L., Fischer A., Bornscheuer U.T., Schmid R.D. Lipase-catalyzed solid phase preparation of sugar fatty acid esters. Biocatal Biotransform. 14:1997;269-283.
45. Bruggink A., Roos E.C., de Vroom E. Penicillin acylase in the industrial production of β-lactam antibiotics. Org Process Res Dev. 2:1998;128-133.
46. Kanda T., Miyata N., Fukui T., Kawamoto T., Tanaka A. Doubly entrapped baker's yeast survives during the long-term stereoselective reduction of ethyl 3-oxobutanoate in an organic solvent. Appl Microbiol Biotechnol. 49:1998;377-381.