Co-immobilization of dextransucrase and dextranase in epoxy-agarose- tailoring oligosaccharides synthesis

[Display omitted] •Agarose-Epoxy support was produced and characterized.•Dextransucrase and dextranase were co-immobilized onto the agarose-epoxy support.•The results were compared to the obtained with Eupergit CM.•The AGE-DS-DN0.5 synthesized oligosaccharides degree of polymerization up to 5.•The i...

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Bibliographic Details
Published in:Process biochemistry (1991) 2019-03, Vol.78, p.71-81
Main Authors: da Silva, Rhonyele Maciel, Paiva Souza, Priscila Maria, Fernandes, Fabiano A.N., Gonçalves, Luciana R.B., Rodrigues, Sueli
Format: Article
Language:English
Subjects:
Bacteria
Catalysis
Co-immobilization
Degree of polymerization
Dextran
Dextranase
Dextransucrase
Economic conditions
Epoxy-agarose
Eupergit CM
Immobilization
Leuconostoc mesenteroides
Oligosaccharides
pH effects
Polymerization
Temperature
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Summary:[Display omitted] •Agarose-Epoxy support was produced and characterized.•Dextransucrase and dextranase were co-immobilized onto the agarose-epoxy support.•The results were compared to the obtained with Eupergit CM.•The AGE-DS-DN0.5 synthesized oligosaccharides degree of polymerization up to 5.•The infrared spectrum showed that Eupergit CM has others reactive groups besides epoxy. The best support reported for dextransucrase (DS) and dextranase (DN) immobilization was Eupergit C, but this carrier was discontinued and is no longer available in the market. Thus, epoxy-agarose support is suggested as an alternative to co-immobilize DS from Leuconostoc mesenteroides B-512F and DN from Chaetomium erraticum. The co-immobilization approach improved DS performance, compared to immobilized DS, due to the removal of the dextran layer accumulated on DS by DN, and enhanced both enzymes catalytic activities under a wide range of pH and temperature. Since DS and DN have the same optimum pH and temperature, the co-immobilization was done in a single step. The EPA-DS-DN0.5 (co-immobilized DS (26.16 UI) and DN (2.76 UI) in epoxy-agarose) showed the highest recovered activity (59.54%). The biocatalyst was stable at 4 °C, retaining above 70% of activity for 60 days and was efficient producing oligosaccharides, yielding 12.68 ± 0.09 g/L of oligosaccharides with a degree of polymerization up to 5.
ISSN:1359-5113
1873-3298
DOI:10.1016/j.procbio.2019.01.009