Abstract
The influence of temperature on the activity of native and immobilized biocatalysts is usually represented in the form of so-called optimum curves (see Fig. 32), in which activity is plotted against temperature. Often, the activity is not given in international units but as the relative activity, i.e., the quotient of the actual activity and the highest activity measured.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Literature
Bourdillon C, Hervagault C, Thomas D (1985) Increase in operational stability of immobilized glucose oxidase by the use of an artificial cosubstrate. Biotechnol Bioeng 27: 1619–1622
Buchholz K (1982) Reaction engineering parameters of immobilized biocatalysts. In: Fiechter A (ed) Advances in biochemical engineering, vol 24. Springer, Berlin Heidelberg New York, pp 39–71
Buchholz K (1983) Parameters involved in heterogeneous biocatalysis. In: Lafferty R M (ed) Enzyme technology. Springer, Berlin Heidelberg New York, pp 9–21
Oagys R J, Pauliukonis A B, Kazlauskas D A (1984) New method for the determination of kinetic constants for two-stage deactivation of biocatalysts. Biotechnol Bioeng 26: 620–622
Davis M E, Watson L T (1985) Analysis of a diffusion-limited hollow fiber reactor for the measurement of effective substrate diffusivities. Biotechnol Bioeng 27: 182–186
Do D D (1985) Determination of Km and De from a one-shot experiment of enzyme immobilization. Biotechnol Bioeng 27: 882–886
Hannoun B J M, Stephanopoulos G (1986) Diffusion coefficients of glucose and ethanol in cell-free and cell-occupied calcium alginate membranes. Biotechnol Bioeng 28: 829–835
Hossain M M, Do D D (1985) Modeling of enzyme immobilization in porous membranes. Biotechnol Bioeng 27: 1126–1135
Juang H-D, Weng H-S (1984) Performance of biocatalysts with nonuniformly distributed immobilized enzymes. Biotechnol Bioeng 26: 623–626
Konecny J (1983) Kinetics and thermodynamics of reactions catalyzed by penicillin acylase-type enzymes. In: Lafferty R M (ed) Enzyme technology. Springer, Berlin Heidelberg New York, pp 309–314
Lenders J-P, Crichton R R (1984) Thermal stabilization of amylolytic enzymes by covalent coupling to soluble polysaccharides. Biotechnol Bioeng 26: 1343–1351
Radovich J M (1985) Mass transfer effects in fermentations using immobilized whole cells. Enzyme Microbial Technol 7: 2–10
Tanaka H, Matsuraura M, Veliky I A (1984) Diffusion characteristics of substrates in Ca-alginate gel beads. Biotechnol Bioeng 26: 53–58
Ulbrich R, Schellenberger A, Daaerau W (1986) Studies on the thermal inactivation of immobilized enzymes. Biotechnol Bioeng 28: 511–522
Vallat I, Nonsan P, Riba J P (1985) Influence of glucose on the kinetics of maltodextrin hydrolysis using free and immobilized glucoamylase. Biotechnol Bioeng 27: 1274–1275
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1988 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Hartmeier, W. (1988). Characteristics of Immobilized Biocatalysts. In: Immobilized Biocatalysts. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73364-2_3
Download citation
DOI: https://doi.org/10.1007/978-3-642-73364-2_3
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-18808-7
Online ISBN: 978-3-642-73364-2
eBook Packages: Springer Book Archive