29 Aug 2016

Immobilization of enzymes in vinyl-sulfone silica

Most methodologies for covalent immobilization of enzymes usually take place at high pH values to enhance the nucleophilicity of protein reactive residues; however, many enzymes inactivate during the immobilization process due to their intrinsic unstability at alkaline pHs. Vinyl sulfone (VS)-activated carriers may react with several protein side-chains at neutral pHs. In this work, levansucrase -an alkaline unstable enzyme of technological interest because it forms fructooligosaccharides (FOS) and levan from sucrose- was covalently attached to VS-activated silica at pH 7.0 in a short time (5 h). The VS-activated biocatalysts showed a notable operational stability in batch reactors. This work was carried out in collaboration with the Department of Organic Chemistry at University of Granada.

Reference: “Vinyl sulfone-activated silica for efficient covalent immobilization of alkaline unstable enzymes: application to levansucrase for fructooligosaccharides synthesis”. P. Santos-Moriano, L. Monsalve-Ledesma, M. Ortega-Muñoz, L. Fernandez-Arrojo, A.O. Ballesteros, F. Santoyo-González, F.J. Plou. RSC Advances 6, 64175–64181 (2016). DOI: 10.1039/C6RA14046G