Literature summary for 3.2.1.B28 extracted from

Kamrat, T.; Nidetzky, B.
Entrapment in E. coli improves the operational stability of recombinant beta-glycosidase CelB from Pyrococcus furiosus and facilitates biocatalyst recovery (2007), J. Biotechnol., 129, 69-76.

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Application

Application	Comment	Organism
synthesis	improvement of the stability of recombinant CelB by entrapment into Escherichia coli cells under conditions promoting strong inactivation. Glutardialdehyde-mediated protein cross-linking or rigidification of the cell membrane by adding magnesium ions is required to prevent release of CelB from within the cell into the bulk solution. In the presence of 1M glucose or when applying recirculation rates of 2.6per min, the entrapped enzyme is around 2fold more stable at 80°C than free CelB. The significance of the stabilisation is attenuated by the decrease in CelB initial activity which wis due to cross-linking and glutardialdehyde concentration-dependent	Pyrococcus furiosus

General Stability

General Stability	Organism
half-life of free enzyme is 680 h in absence and 22 h in presence of 1 M glucose, half-life of cross-linked enzyme is 18 h in absence and 3 h in presence of 1 M glucose, half-life of cross-linked cells is 840 h in absence and 47 h in presnce of 1 M glucose, respectively	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	Q51723	-	-

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Release 2023.1 (January 2023)