Control of an affinity purification procedure using a thermal biosensor
- 5 October 1990
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 36 (7) , 723-726
- https://doi.org/10.1002/bit.260360710
Abstract
Lactate dehydrogenase (LDH) was recovered from a solution by affinity binding to an N6‐(6‐aminohexyl)‐AMP‐Sepharose gel. An enzyme thermistor unit was employed to continously measure the activity of the unbound LDH. The enzyme activity signal from the enzyme thermistor was used in a PID controller to regulate the addition of AMP‐Sepharose gel to the LDH solution. In another type of experiment, a desktop computer was utilized to control the addition of the adsorbent. Both systems worked satisfactorily, and enabled a rapid and accurate assessment of correct addition of adsorbent.This publication has 6 references indexed in Scilit:
- [11] Hybrid biosensors for clinical analysis and fermentation controlPublished by Elsevier ,1988
- Monitoring and control of enzymic sucrose hydrolysis using on-line biosensorsApplied Microbiology and Biotechnology, 1985
- Fermented foods, feeds and beveragesBiotechnology Advances, 1983
- Evaluation of the enzyme thermistor as a specific detector for chromatographic proceduresAnalytical Biochemistry, 1981
- Determination of enzyme activities with the enzyme thermistor unitFEBS Letters, 1979
- [16] AMP and NAD as “general ligands”Published by Elsevier ,1974