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 are aldehydes as several studies in animals indicate that they can be mutagenic, carcinogenic, cytotoxic and genotoxic. 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 potentially toxic compounds, one of which is aldehyde dehydrogenase enzyme superfamily.
As mouth is the first part of the 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 for aromatic aldehydes commonly found in food. However, because of hyposalvation, 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 occuring in food products (vanillin, citral, furfural, cinnamaldehyde, anisaldehyde, benzaldehyde and hexenal) were determined by measuring the increase of NADH fluorescence after adding different concentrations of aldehyde substrates. Rates were used to construct the Lineweaver - Burk plot form which Km and Vmax values were calculated.
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 enzyme. Thus supporting role of ALDH1A1 in the protection of organisms against these potentially dangerous compounds from food can be suggested.

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