(1) Instituto de Catálisis, CSIC, Campus UAM Cantoblanco, 28049 Madrid, Spain;(2) Centre de Bioingénierie Gilbert Durand, UMR CNRS 5504, LA INRA, INSA, Complexe Scientifique de Rangueil, 331077 Toulouse cedex, France
Abstract:
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.