Acrolein detection based on alcohol dehydrogenase inhibition

Abstract

This paper presents the effect of acrolein on three dehydrogenases and proposes a fast spectrometric method for acrolein analysis. We have found that alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (AlDH) are inhibited by low acrolein concentrations (0.2 mM) while inhibition of glutamate dehydrogenase (GDH) is not observed even at higher acrolein concentrations (1 mM). Acrolein is a suicide substrate for AlDH and ADH inhibition by acrolein is competitive. Cysteine (L-Cys) and glutathione (GSH) react with acrolein and thus reduce its expected inhibitory effect. ADH was chosen to develop a spectrophotometric method for acrolein analysis based on enzyme inhibition. The calibration curve is linear between 0.2 and 1.0 mM acrolein.

Keywords:

• acrolein inhibition
• acrolein analysis
• alcohol dehydrogenase
• aldehyde dehydrogenase
• glutamate dehydrogenase

Acknowledgements

This work was supported by Romanian Ministry of Education and Research UEFISCDI (projects PN II-RU TE-100/2010 and BLUEBOXSENS 82102/2008). Ovidiu Ilie Covaci is a Ph.D. student with a scholarship funded by the Sectoral Operational Programme Human Resources Development 2007-2013 of the Romanian Ministry of Labour, Family and Social Protection through the Financial Agreement POSDRU/6/1.5/S/19. Paper revision by Dr Alina Vasilescu is gratefully acknowledged.