Enzyme Technology
Summary and Bibliography of Chapter 3
- Immobilisation of enzymes enables their efficient
and continuous use. The rationale behind immobilisation is the easy separation
of product from the biocatalyst.
- Enzymes may be immobilised by
adsorption, covalent binding, entrapment and membrane confinement, each method
having its pros and cons. Adsorption is quick, simple and cheap but may be
reversible. Covalent binding is permanent but expensive. Entrapment is generally
applicable but may cause diffusional problems. Membrane confinement is a
flexible method but expensive to set up.
- Immobilisation of enzymes may
have a considerable effect on their kinetics. This may be due to structural
changes to the enzyme and the creation of a distinct microenvironment around the
enzyme. The activity of an immobilised enzyme is governed by the physical
conditions within this microenvironment not those prevalent in the bulk phase.
The immobilisation matrix affects the partition of material between the product
phase and the enzyme phase and imposes restrictions on the rate of diffusion of
material.
- Some effects of enzyme immobilisation are seen to be
beneficial while others are detrimental to the economics of their use.
References and Bibliography
- Bodálo, A., Gómez, J.L., Gómez, E., Bastida, J., Iborra,
J.L. & Manjón, A. (1986). Analysis of diffusion effects on immobilized
enzymes on porous supports with reversible Michaelis-Menten kinetics. Enzyme
and Microbial Technology8, 433-8.
- Engasser, J-M. & Coulet, P.R. (1977). Comparison
of intrinsic stabilities of free and bound enzymes by graphical removal of
diffusional effects. Biochimica et Biophysica Acta 485, 29-36.
- Engasser, J-M. & Horvath,
C. (1973). Effect of internal diffusion in heterogeneous enzyme systems: Evaluation
of true kinetic parameters and substrate diffusivity. J. Theoretical
Biology 42, 137-55.
- Engasser, J-M. & Horvath, C. (1974). Buffer-facilitated
proton transport pH profile of bound enzymes. Biochimica et Biophysica
Acta 358 178-92.
- Engasser, J-M. & Horvath, C. (1976). Diffusion and
kinetics with immobilised enzymes. In Applied biochemistry and bioengineering,
vol. 1 Immobilised enzyme principles. ed. L.B.Wingard,
- E.Katchalski-Katzir & L.Goldstein, pp 127-220, New
York: Academic Press.European Federation of Biotechnology (1983). Guidelines
for the characterization of immobilised biocatalysts. Enzyme and Microbial
Technology 5, 304-7.
- Goldstein, L. (1972). Microenvironmental
effects on enzyme catalysis. A kinetic study of polyanionic and polycationic
derivatives of chymotrypsin. Biochemistry, 11, 4072-84.
- Israelachvili, J. & Pashley, R. (1982). The hydrophobic
interaction is long range, decaying exponentially with distance. Nature,
300 341-2.
- Kennedy, J.F. & Cabral, J.M.S., (1987). Enzyme immobilisation.
In Biotechnology, vol. 7a, Enzyme Technology, ed. J.F.Kennedy, pp 347-404.
Weinheim: VCH Verlagsgesellschaft mbH.
- Martinek, K., Klibanov, A.M.,
Goldmacher, V.S. & Berezin, I.V. (1977a). The principles of enzyme stabilization
1. Increase in thermostability of enzymes covalently bound to a complementary
surface of a polymer support in a multipoint fashion. Biochimica et Biophysica
Acta, 485, 1-12.
- Martinek, K., Klibanov, A.M.,
Goldmacher, V.S., Tchernysheva, A.V., Mozhaev, V.V., Berezin, I.V. & Glotov,
B.O. (1977b). The principles of enzyme stabilization 2. Increase in the thermostability
of enzymes as a result of multipoint noncovalent interaction with a polymeric
support. Biochimica et Biophysica Acta 485, 13-28.
- Woodward, J. (1985). Immobilised
enzymes: Adsorption and covalent coupling. In Immobilised cells and enzymes
A practical approach, ed. J.Woodward, pp 3-17. Oxford: IRL Press Ltd.
- Working party on immobilised biocatalysts. (1983). Guidelines
for the characterization of immobilised biocatalysts. Enzyme and Microbial
Technology, 5, 304-307.
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