Bioluminescent biosensors bioluminescence analysis

However, native bioluminescent enzymes are generally subject to inactivation in vitro, and hence not suitable for routine analytical use. Immobilized enzymes and whole bacteria largely solve this instability problem, and hence enable the routine use of bioluminescent analysis with high speed, specificity, simplicity, sensitivity and accuracy. Inunobilization also enables the development of automated luminescent biosensors. 

Bacterial luciferase coimmobilized with NAD(P)H FMN oxidoreductase on starch gel has been used for bioluminescent assay of aldehydesCo-immobilization of bacterial luciferase, NAD(P)H FMN oxidoreductase and their substrates is referred to as multifunctional immobilized biosensor and is a new trend for use of bioluminescent analysis, e.g. toxicity biotest and bioassay. The main principle of this luciferase biotest is the correlation between toxicity of the sample being studied and changes in bioluminescence parameters in vitro. Toxicity of the sample is measured by the changes in bioliuninescence intensity compared with that of a control. Multifunctional immobilized biosensors based on luciferase have been used for the following bioassays. 

Simoni P, Baraldini M. Bioluminescent biosensors based on 60. genetically engineered living cells in environmental and food analysis. Analytical Lett. 2006 39 1503-1515. 

The effect of blood serum, lymph and other biological liquids on bioluminescent reactions has been studied. The immobilized luciferase shows lower sensitivity than the soluble enzyme in human clinical tests, and in analysis of com and bread infection by fungi. But this problem is overcome by using larger samples, and hence this new biosensor can be successfully used for toxicity bioassays. 

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