Improvement of a beta-glucanase activity test by taking into account the batch reactor balance of the test system.
Activity tests of enzymes are often applied for determining their concentration. In the easiest case, just one product concentration is measured after a given time. This often leads to nonlinear dependences of the apparent activity with enzyme protein concentration. A general solution of this problem consists in using the balance equation of the assay system, which commonly represents a batch reactor. Here, the balance equation of the batch for a general Michaelis Menten-type reaction kinetics is used as the calibration function. The correlation of the apparent activity and enzyme concentration was established by capturing the enzyme by means of metal chelate interaction owing to a hexahistidine tag attached to the beta-glucanase.
Beshay
Usama
U
Faculty of Technology, Fermentation Engineering, Bielefeld University, Bielefeld 33594, Germany.
Miksch
Gerd
G
Flaschel
Erwin
E
D019149:Bioreactors / Q000382:microbiology*; D002623:Chemistry Techniques, Analytical / Q000379:methods*; D004789:Enzyme Activation; D004867:Equipment Design; D019544:Equipment Failure Analysis; D004926:Escherichia coli / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000032:analysis* / Q000737:chemistry*; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity
D006026:Glycoside Hydrolases; C028020:licheninase