EC Number |
Title |
Organism |
---|
3.2.1.B28 | An L213A variant of beta-glycosidase from Sulfolobus solfataricus with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to compound K |
Pyrococcus furiosus |
3.2.1.B28 | Activity and stability of hyperthermophilic enzymes: a comparative study on two archaeal beta-glycosidases |
Pyrococcus furiosus |
3.2.1.B28 | Activity of hyperthermophilic glycosynthases is significantly enhanced at acidic pH |
Pyrococcus furiosus |
3.2.1.B28 | Characterization of the celB gene coding for beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli |
Pyrococcus furiosus |
3.2.1.B28 | Comparative structural analysis and substrate specificity engineering of the hyperthermostable beta-glucosidase CelB from Pyrococcus furiosus |
Pyrococcus furiosus |
3.2.1.B28 | Continuous production of lactulose by immobilized thermostable beta-glycosidase from Pyrococcus furiosus |
Pyrococcus furiosus |
3.2.1.B28 | Denaturation of an extremely stable hyperthermophilic protein occurs via a dimeric intermediate |
Pyrococcus furiosus |
3.2.1.B28 | Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable beta-glycosidases |
Pyrococcus furiosus |
3.2.1.B28 | Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. III. Utilization of two thermostable beta-glycosidases in a continuous ultrafiltration membrane reactor and galacto-oligosaccharide formation under steady-state conditions |
Pyrococcus furiosus |
3.2.1.B28 | Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable beta-glycosidases and optimization of a packed-bed reactor for lactose conversion |
Pyrococcus furiosus |