title: Contribution of ALDH1A1 isozyme to detoxification of aldehydes present in food products.
abstract: Even though food awareness is so developed and more and more people pay attention to what their diet is composed of, it is not possible to exclude all potentially dangerous substances present in our diet. One group of such compounds may be aldehydes as several studies indicate that they can be mutagenic, carcinogenic, genotoxic and cytotoxic. These relatively reactive organic molecules are natural constituents of food. They are also extensively used by food industry as additives giving aroma and taste. Fortunately many enzyme systems were developed to protect us against these toxic compounds, one of which is aldehyde dehydrogenase enzyme superfamily. As mouth is the first part of digestive system it seems crucial for detoxifying toxic substances introduced with our diet. The only ALDH isozyme present in saliva is ALDH3A1, which has very high affinity towards aromatic aldehydes commonly found in food. However, because of hyposalivation, which is not uncommon nowadays, the effectiveness of this barrier can be drastically diminished. As another member of this enzyme family, isozyme ALDH1A1 is also present in digestive system its possible contribution to detoxification of "food" aldehydes was addressed. Kinetic parameters (Km, Vmax) of recombinant ALDH1A1 towards several aliphatic and aromatic aldehydes occurring in food products (vanillin, citral, furfural, cinnamaldehyde, anisaldehyde, benzaldehyde and trans-hexenal) were determined by measuring the increase of NADH fluorescence after adding various concentrations of aldehyde substrates. Rates were used to construct the Lineweaver-Burk plot from which Km and Vmax (measured relative to that of benzaldehyde which was assigned the value of 100) values were calculated. The following results were obtained: 0.04 +/- 0.06 microM and 277 +/- 81 for anisaldehyde, 0.86 +/- 0.03 mciroM and 50 +/- 3 for vanillin, 0.18 +/- 0.05 mciroM and 93 +/- 9 for trans-2-hexenal, 0.17 +/- 0.03 microM and 201 +/- 32 for cinnamaldehyde, 5.8 +/- 0.3 mciroM and 281 +/- 59 for furfural, 0.65 +/- 0.05 microM and 139 +/- 9 for citral, 0.4 +/- 0.2 microM and 100 for benzaldehyde. It turned out that this ubiquitous member of ALDHs superfamily, has very good affinity for examined aldehydes. The resulting Michaelis - Menten constant values are even lower than the corresponding values for ALDH3A1 enyzme. Thus supporting role of ALDH1A1 in the protection of organisms against these dangerous compounds from food can be suggested.
authors.affiliation: Department of Bioanalysis and Drug Analysis, Faculty of Pharmacy, Warszawa, Poland.
authors.forename: Sylwia
authors.initials: S
authors.lastname: Sołobodowska
authors.forename: Joanna
authors.initials: J
authors.lastname: Giebułtowicz
authors.forename: Renata
authors.initials: R
authors.lastname: Wolinowska
authors.forename: Piotr
authors.initials: P
authors.lastname: Wroczyński
mesh_terms: D000444:Aldehyde Dehydrogenase / Q000502:physiology*; D000080924:Aldehyde Dehydrogenase 1 Family; D000447:Aldehydes / Q000378:metabolism*; D005503:Food Additives / Q000378:metabolism*; D006801:Humans; D008658:Inactivation, Metabolic; D050697:Retinal Dehydrogenase
chemical_list: D000447:Aldehydes; D005503:Food Additives; D000080924:Aldehyde Dehydrogenase 1 Family; D000444:Aldehyde Dehydrogenase; C510223:ALDH1A1 protein, human; D050697:Retinal Dehydrogenase