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Merck

Enhanced stability of Bacillus licheniformis L-arabinose isomerase by immobilization with alginate.

Preparative biochemistry & biotechnology (2009-12-22)
Ye-Wang Zhang, Ponnandy Prabhu, Jung-Kul Lee, In-Won Kim
RESUMO

Recombinant Escherichia coli whole cells harboring Bacillus licheniformis L-arabinose isomerase (BLAI) were harvested to prepare alginate-immobilized biocatalysts. The operational conditions for immobilization were optimized according to relative activity and the cell leakage of the immobilized cell. The optimal conditions are as follows: alginate concentration, Ca(2+) concentration, cell mass loading, and curing time were 2% (w/v), 0.1 M, 50 g l(-1), and 4 hours, respectively. After immobilization, cross-linking with 0.1% glutaraldehyde significantly reduced cell leakage. The immobilized whole cells harboring BLAI were very stable with 89% residual activity remaining after 33 days of incubation at 50 degrees C and were much more stable than the free enzyme and cells. The results showed that immobilizing whole cells harboring BLAI is suitable for use as a biocatalyst in the production of L-ribulose, largely due to its high stability and low cost.

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Sigma-Aldrich
L-Ribulose, ≥90% (HPLC)
Sigma-Aldrich
D-Ribulose solution, ~1 M in H2O, ≥97.0% (HPLC)