title: The use of tomato aminoaldehyde dehydrogenase 1 for the detection of aldehydes in fruit distillates.
abstract: Plant NAD(+)-dependent aminoaldehyde dehydrogenases (AMADHs, EC 1.2.1.19) belong to the family 10 of aldehyde dehydrogenases. They participate in the metabolism of polyamines or osmoprotectants. The enzymes are characterized by their broad substrate specificity covering ω-aminoaldehydes, aliphatic and aromatic aldehydes as well as nitrogen-containing heterocyclic aldehydes. The isoenzyme 1 from tomato (Solanum lycopersicum; SlAMADH1) oxidizes aliphatic aldehydes very efficiently and converts also furfural, its derivatives or benzaldehyde, which are present at low concentrations in alcoholic distillates such as fruit brandy. In this work, SlAMADH1 was examined as a bioanalytical tool for their detection. These aldehydes arise from fermentation processes or thermal degradation of sugars and their presence is related to health complications after consumption including nausea, emesis, sweating, decrease in blood pressure, hangover headache, among others. Sixteen samples of slivovitz (plum brandy) from local producers in Moravia, Czech Republic, were analyzed for their aldehyde content using a spectrophotometric activity assay with SlAMADH1. In all cases, there were oxidative responses observed when monitoring NADH production in the enzymatic reaction. Aldehydes in the distillate samples were also subjected to a standard determination using reversed-phase HPLC with spectrophotometric and tandem mass spectrometric detection after a derivatization with 2,4-dinitrophenylhydrazine. Results obtained by both methods were found to correlate well for a majority of the analyzed samples. The possible applicability of SlAMADH1 for the evaluation of aldehyde content in food and beverages has now been demonstrated.
authors.affiliation: Department of Protein Biochemistry and Proteomics, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University, Šlechtitelů 27, 783 71 Olomouc, Czech Republic.
authors.forename: Jan
authors.initials: J
authors.lastname: Frömmel
authors.affiliation: Central Laboratories and Research Support, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University, Šlechtitelů 27, 783 71 Olomouc, Czech Republic.
authors.forename: Petr
authors.initials: P
authors.lastname: Tarkowski
authors.affiliation: Department of Protein Biochemistry and Proteomics, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University, Šlechtitelů 27, 783 71 Olomouc, Czech Republic.
authors.forename: David
authors.initials: D
authors.lastname: Kopečný
authors.affiliation: Department of Protein Biochemistry and Proteomics, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University, Šlechtitelů 27, 783 71 Olomouc, Czech Republic. Electronic address: marek.sebela@upol.cz.
authors.forename: Marek
authors.initials: M
authors.lastname: Šebela
mesh_terms: D000434:Alcoholic Beverages / Q000009:adverse effects / Q000032:analysis*; D000080924:Aldehyde Dehydrogenase 1 Family; D000447:Aldehydes / Q000009:adverse effects / Q000032:analysis*; D001709:Biotechnology; D002851:Chromatography, High Pressure Liquid; D057168:Distillation; D005638:Fruit / Q000737:chemistry; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D018551:Solanum lycopersicum / Q000201:enzymology*; D010940:Plant Proteins / Q000378:metabolism*; D000068242:Prunus domestica / Q000737:chemistry; D050697:Retinal Dehydrogenase / Q000378:metabolism*; D053719:Tandem Mass Spectrometry
chemical_list: D000447:Aldehydes; D007527:Isoenzymes; D010940:Plant Proteins; D000080924:Aldehyde Dehydrogenase 1 Family; C510223:ALDH1A1 protein, human; D050697:Retinal Dehydrogenase