Discovery of a Bacterial Gene Cluster for Deglycosylation of Toxic Potato Steroidal Glycoalkaloids α-Chaconine and α-Solanine

TY - JOUR

T1 - Discovery of a Bacterial Gene Cluster for Deglycosylation of Toxic Potato Steroidal Glycoalkaloids α-Chaconine and α-Solanine

AU - Hennessy, Rosanna C.

AU - Nielsen, Søren D.

AU - Greve-Poulsen, Mathias

AU - Larsen, Lotte Bach

AU - Sørensen, Ole Bandsholm

AU - Stougaard, Peter

PY - 2020

Y1 - 2020

N2 - 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.

AB - 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.

KW - Arthrobacter

KW - glycoalkaloids degradation

KW - human nutrition

KW - potato proteins

KW - solanidine

KW - α-chaconine

KW - α-rhamnosidase

KW - α-solanine

KW - β-galactosidase

KW - β-glucosidase

UR - http://www.scopus.com/inward/record.url?scp=85079022617&partnerID=8YFLogxK

U2 - 10.1021/acs.jafc.9b07632

DO - 10.1021/acs.jafc.9b07632

M3 - Journal article

C2 - 31935098

AN - SCOPUS:85079022617

SN - 0021-8561

VL - 68

SP - 1390

EP - 1396

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 5

ER -