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Control of an affinity purification procedure using a thermal biosensor
Author(s) -
Flygare Lilian,
Larsson PerOlof,
Danielsson Bengt
Publication year - 1990
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260360710
Subject(s) - thermistor , sepharose , chromatography , lactate dehydrogenase , adsorption , biosensor , chemistry , enzyme , affinity chromatography , immobilized enzyme , specific activity , biochemistry , organic chemistry , engineering , electrical engineering
Lactate dehydrogenase (LDH) was recovered from a solution by affinity binding to an N 6 ‐(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.