원문정보
초록
영어
A thermostable α-L-arabinofuranosidases (α-L-AFase) is an industrially important enzyme for recovery of Larabinose from hemicellulose. The recombinant α-L-AFase from Thermotoga maritima was expressed in Escherichia coli by using a constitutive pHCE or an inducible pRSET vectors. In batch fermentation, the constitutive expression system resulted in slightly faster growth rate (0.78 vs. 0.74/hr) but lower enzyme activity (2,553 vs. 3,723 units/L) than those of the induction system. When fed-batch fermentation was performed, biomass and enzyme activity reached the highest levels of 36 g/L and 9,152 units/L, respectively. The fed batch cultures performed superior results than batch culture in terms of biomass yield (4.62-5.42 folds) and enzyme synthesis (3.39-4.00 folds). In addition, the fed-batch induction strategy at high cell density resulted in the best productivity in cell growth as well as enzyme activity rather than the induction method at low cell density or the constitutive expression.
목차
Introduction
Materials and Methods
Bacterial strains and plasmids
Culture and media
Batch and fed-batch fermentation
Analytical methods
Results and Discussion
Batch culture and protein analysis
Fed-batch culture with constitutive expression
Fed-batch culture by induction at low cell density
Fed-batch culture by induction at high cell density
References