Abstract
The enzymatic assay for pyruvate using soluble lactate dehydrogenase (LDH) by flow injection analysis (FIA) has been investigated. Using a 50-cm knitted open tubular reactor (KOT), it was found that plate height ( H) decreased by a factor of 4 as the flow rate went down from 100 to 10 μl/min. A corresponding increase in peak height by a factor of 6 was also seen over this flow rate range. To stabilize the LDH activity, polyethylene glycol (PEG) was added to the reagent solution, extending the enzyme lifetime to at least a week. The presence of PEG in solution stabilized LDH activity better than the use of covalently bound PEG-LDH enzyme. A linear pyruvate range from 0.01 to 0.75 m M was established with a sample throughput of about 330 s per sample at 10 μl/min.
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