Dextransucrase immobilized on activated-chitosan particles as a novel biocatalyst

Publication date: Available online 14 December 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Natália G. Graebin, Diandra de Andrades, Marina C. Bonin, Rafael C. Rodrigues, Marco A.Z. Ayub Dextransucrase from Leuconostoc mesenteroides B-512F was covalently immobilized on glutaraldehyde-actived chitosan particles. The best initial protein loading (400mg/g of dried support) showed 197U/g of catalytic activity. The optimal reaction pH and temperature of this new biocatalyst were determined to be 4.5 and 20°C, respectively. Regarding the thermal stability, the immobilization enhanced enzyme protection against high temperatures, whereas glucose and maltose acted as stabilizers. The biocatalyst was stable under storage at 5°C for a month. The biocatalyst presented good operational stability, retaining up to 40% of its initial activity after ten batch cycles of reaction to obtain oligosaccharides. These results suggest the use of the immobilized dextransucrase on chitosan particles as a promising novel biocatalyst to produce dextran and oligosaccharides. Graphical abstract

Source: Journal of Molecular Catalysis B: Enzymatic - December 13, 2016 Category: Biochemistry Source Type: research