Open AccessHorseradish Peroxidase Combined With Oxidase Enzymes a Valuable Bioanalytical Tool: Lactate Oxidase – A Case Study
Author(s) -
Vojinovic V.,
Bertin L.,
Cabral J. M. S.,
Fonseca L. P.
Publication year - 2006
Publication title -
engineering in life sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.547
H-Index - 57
eISSN - 1618-2863
pISSN - 1618-0240
DOI - 10.1002/elsc.200620908
Subject(s) - bioprocess , bioanalysis , biosensor , glucose oxidase , horseradish peroxidase , chemistry , peroxidase , biochemistry , oxidase test , enzyme , combinatorial chemistry , chromatography , chemical engineering , engineering
Enzymatic biosensors have been extensively investigated for real‐time bioprocess monitoring and other online analysis. However, implementation of biosensors has been strongly hindered by their limited stability. This work reports a significant improvement of the stability of the immobilized oxidases by in situ reduction of the harmful H 2 O 2 . Thus, stabilized oxidases can serve as the basis for ethanol, glucose, and lactate sensors, with the ability to operate for long periods of time with virtually no change in activity. As an example, a lactate sensor, containing lactate oxidase aimed for bioprocess monitoring, has been described and characterized. Operational stabilities that allow up to 8 h continuous lactate conversion with virtually no activity loss have been achieved. The described system based on the in situ stabilization strategy is a promising new tool for the development of online analyses.