Discovery of a Bacterial Gene Cluster for Deglycosylation of Toxic Potato Steroidal Glycoalkaloids α-Chaconine and α-Solanine
Rosanna C. Hennessy, Søren Drud-Heydary Nielsen, Mathias Greve-Poulsen, Lotte Bach Larsen, Ole Bandsholm Sørensen, Peter Stougaard
Abstract
Potato juice is a byproduct of starch processing currently used as feed. However, potato proteins are an untapped source of high-protein food for human nutrition if harmful constituents notably glycoalkaloids (GAs) are detoxified. The two principle GAs found in potato are α-chaconine and α-solanine, both consisting of a solanidine aglycone with a carbohydrate side chain. The first step in the detoxification of these compounds is the removal of the trisaccharide. Whole-genome sequencing of a bacterial isolate, Arthrobacter sp. S41, capable of completely degrading α-chaconine and α-solanine, revealed the presence of a gene cluster possibly involved in the deglycosylation of GAs. Functional characterization confirmed the enzymatic activity of the gene cluster involved in the complete deglycosylation of both α-chaconine and α-solanine. The novel enzymes described here may find value in the bioconversion of feed proteins to food proteins suitable for human nutrition.