The gene encoding β-glycosidase of the hyperthermophilic archaea Sulfolobus shibatae (SSG) was expressed in Escherichia coli. Recombinant SSG (referred to as rSSG hereafter) was efficiently purified, and its transglycosylation activity was tested with lactose as a donor and various sugars as acceptors. When sucrose was used as an acceptor, we found a distinct intermolecular transglycosylation product and confirmed its presence by TLC and high performance anion exchange chromatography (HPAEC). The sucrose transglycosylation product was isolated by paper chromatography, and its chemical structure was determined by 1H and 13C NMR. The sucrose transfer product was determined to be β-d-galactopyranosyl- (1→6)-α-d-glucopyranosyl-β-d-fructofuranoside with a galactose molecule linked to sucrose via a β-(1→6)-glycosidic bond.
Bibliographical noteFunding Information:
This study was supported by Korea Research Foundation (2003-042-F20015). The authors are grateful to Dr. Nelly Tsvetkova for critically reading the manuscript.
All Science Journal Classification (ASJC) codes
- Analytical Chemistry
- Organic Chemistry