α-Glucosidase from Pyrococcus furiosus

Hyperthermophilic α-glucosidases could also provide valuable insights into protein function, structure, and stability at high temperatures. Indeed, it is the intrinsic high temperature activity and stability of these proteins that have fueled considerable effort into the development of these and other glycosylhydrolases for use in starch conversion technology. Currently employed mesophilic enzymes exhibit limited tolerance to the high temperatures and pH variations encountered during starch solubilization and degradation. These mesophilic enzymes often have metal ion requirements for activity, whereas their counterpart hyperthermophilic versions often do not. Although pullulanases and glucoamylases (also known as amyloglucosidases) are typically used for saccharification of intermediate starch degradation products to glucose, heat-stable α-glucosidases, together with pullulanases, could theoretically fill that role more efficiently. However, despite the potential impact of hyperthermophilic enzymes on industrial processes, including starch conversion, their application is still largely unrealized. One readily apparent obstacle is developing a costefficient method for producing sufficient quantities of enzyme either directly from the source organism or through recombinant means.