کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
25254 43563 2007 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Entrapment in E. coli improves the operational stability of recombinant β-glycosidase CelB from Pyrococcus furiosus and facilitates biocatalyst recovery
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Entrapment in E. coli improves the operational stability of recombinant β-glycosidase CelB from Pyrococcus furiosus and facilitates biocatalyst recovery
چکیده انگلیسی

β-Glycosidase CelB from the hyperthermophilic archaeon Pyrococcus furiosus is a versatile biocatalyst that has been used for the hydrolysis and synthesis of β-d-glycosidic compounds at high temperatures and in non-conventional solvents. In spite of its outstanding thermal stability, CelB is prone to inactivation in the presence of reducing sugars and through recirculation in loop enzyme reactors. Entrapment into E. coli cells was used here to improve the stability of recombinant CelB under conditions promoting strong inactivation. Glutardialdehyde-mediated protein cross-linking or rigidification of the cell membrane by adding magnesium ions was required to prevent release of CelB from within the cell into the bulk solution. In the presence of 1 M glucose or when applying recirculation rates of 2.6 min−1, the entrapped enzyme was around two-fold more stable at 80 °C than free CelB. The significance of the stabilisation was attenuated by the decrease in CelB initial activity which was due to cross-linking and glutardialdehyde concentration-dependent. Entrapment facilitated downstream processing of CelB and biocatalyst recovery in repeated batchwise conversions of lactose at elevated temperatures.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Biotechnology - Volume 129, Issue 1, 30 March 2007, Pages 69–76
نویسندگان
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