Biochemical Engineering Journal, Год журнала: 2025, Номер unknown, С. 109794 - 109794
Опубликована: Май 1, 2025
Язык: Английский
Biochemical Engineering Journal, Год журнала: 2025, Номер unknown, С. 109794 - 109794
Опубликована: Май 1, 2025
Язык: Английский
ACS Synthetic Biology, Год журнала: 2025, Номер unknown
Опубликована: Апрель 15, 2025
The subunit dissociation of oligomeric enzymes is a major challenge that limits their practical applications. In this study, yeast-surface-displayed tetrameric β-glucuronidase with C-terminal anchor protein fusion was found partially dissociated into dimers. coexpression free and anchored subunits significantly improved the display efficiency catalytic activity. Given may adopt non-native conformation on cell surface, interfaces surface-displayed were in situ characterized using Förster resonance energy transfer (FRET) strategy, structure well maintained coexpressed β-glucuronidases. Finally, strategy applied to cellulases, enhancing activities endoglucanase dimeric β-glucosidase concentration cellulosic ethanol for two-enzyme codisplaying strain. This work provides insights structure-activity relationship efficient utilization enzymes.
Язык: Английский
Процитировано
0Biochemical Engineering Journal, Год журнала: 2025, Номер unknown, С. 109794 - 109794
Опубликована: Май 1, 2025
Язык: Английский
Процитировано
0