Modeling Trienzyme Biosensor at Internal Diffusion Limitation

2004 ◽  
Vol 9 (2) ◽  
pp. 139-144 ◽  
Author(s):  
J. Kulys
Keyword(s):  
Immobilized Enzymes ◽  
Internal Diffusion ◽  
Significant Response ◽  
Diffusion Limitation ◽  
Enzyme Reactions ◽  
Substrate Conversion ◽  
Apparent Stability ◽  
Biosensor Response

A model of biosensor containing three immobilized enzymes utilizing consecutive substrate conversion in the chain was developed. The modeling was performed at an internal diffusion limitation and a steadystate condition. The calculations showed that significant response of biosensors was produced if diffusion modules were larger than 1 for all enzyme reactions. Due to diffusion limitation the apparent stability of biosensor response increased many times in comparison to stability of the most labile enzyme of the chain.

Effects of internal diffusion on the lineweaver-Burk plots for immobilized enzymes

1975 ◽  
Vol 17 (3) ◽  
pp. 423-431 ◽  
Author(s):  
Shinichiro Gondo ◽  
Shogo Isayama ◽  
Koichiro Kusunoki
Keyword(s):  
Immobilized Enzymes ◽  
Internal Diffusion

scholarly journals Semi-Continuous Flow Biocatalysis with Affinity Co-Immobilized Ketoreductase and Glucose Dehydrogenase

Molecules ◽  
2020 ◽  
Vol 25 (18) ◽  
pp. 4278
Author(s):  
Michal Plž ◽  
Tatiana Petrovičová ◽  
Martin Rebroš
Keyword(s):  
Substrate Concentration ◽  
Continuous Flow ◽  
Flow Reactor ◽  
Glucose Dehydrogenase ◽  
Immobilized Enzymes ◽  
Significant Enhancement ◽  
Hydroxy Ketone ◽  
N Terminus ◽  
Substrate Conversion ◽  
Affinity Interaction

The co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) was studied. Immobilization of these two enzymes was performed via affinity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes were applied in a semicontinuous flow reactor to convert the model substrate; α-hydroxy ketone. A series of biotransformation reactions with a substrate conversion of >95% were performed. Immobilization reduced the requirement for cofactor (NADP+) and allowed the use of higher substrate concentration in comparison with free enzymes. The immobilized system was also tested on bulky ketones and a significant enhancement in comparison with free enzymes was achieved.

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