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Immobilization of native and dextran-free dextransucrases from Leuconostoc mesenteroides NRRL B-512F for the synthesis of glucooligosaccharides

Dextransucrase from Leuconostoc mesenteroides NRRL B-512F was immobilized using two different methods: covalent attachment to activated silica and entrapment in calcium alginate. For immobilization on silica, native enzyme and dextran-free enzyme were compared. However, the entrapment in calcium alg...

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Bibliographic Details
Published in:Biotechnology techniques 1999-11, Vol.13 (11), p.749-755
Main Authors: ALCALDE, M, PLOU, F. J, GOMEZ DE SEGURA, A, REMAUD-SIMEON, M, WILLEMOT, R. M, MONSAN, P, BALLESTEROS, A
Format: Article
Language:English
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Summary:Dextransucrase from Leuconostoc mesenteroides NRRL B-512F was immobilized using two different methods: covalent attachment to activated silica and entrapment in calcium alginate. For immobilization on silica, native enzyme and dextran-free enzyme were compared. However, the entrapment in calcium alginate beads gave the best results in terms of immobilization yield and stability. This biocatalyst was employed in the acceptor reaction with maltose showing similar glucooligosaccharide production than the native enzyme but increased operational stability.
ISSN:0951-208X
1573-6784
DOI:10.1023/A:1008966213425