Larissa Lemos Faria1, Sergio Andres Villalba Morales1, José Pedro Zanetti Prado1, Giancarlo de Souza Dias1, Alex Fernando de Almeida2, Michelle da Cunha Abreu Xavier2, Elda Sabino da Silva3, Alfredo Eduardo Maiorano3, Rafael Firmani Perna4. 1. Institute of Science and Technology, Federal University of Alfenas (UNIFAL-MG), José Aurélio Vilela Road 11999, Km 533, Poços de Caldas, MG, Zip Code 37715-400, Brazil. 2. Department of Bioprocess Engineering and Biotechnology, Federal University of Tocantins (UFT), Badejos Street 69-72, Jardim Cervilha, Gurupi, TO, Zip Code 77404-970, Brazil. 3. Bionanomanufacturing Center, Institute for Technological Research (IPT-SP), Av. Prof. Almeida Prado 532, University City, São Paulo, SP, Zip Code 05508-901, Brazil. 4. Institute of Science and Technology, Federal University of Alfenas (UNIFAL-MG), José Aurélio Vilela Road 11999, Km 533, Poços de Caldas, MG, Zip Code 37715-400, Brazil. rafael.perna@unifal-mg.edu.br.
Abstract
OBJECTIVE: Extracellular fructosyltransferase (FTase, E.C.2.4.1.9) from Aspergillus oryzae IPT-301 was immobilized on silica gel by adsorption and biochemically characterized aiming at its application in the transfructosylation reaction of sucrose for the production of fructooligossaccarides (FOS). RESULTS: The transfructosylation activity (AT) was maximized by the experimental design in function of the reaction pHs and temperatures. The AT of the immobilized enzyme showed the kinetics behavior described by the Hill model. The immobilized FTase showed reuse capacity for six consecutive reaction cycles and higher pH and thermal stability than the soluble enzyme. CONCLUSION: These results suggest a high potential of application of silica gel as support for FTase immobilization aiming at FOS production.
OBJECTIVE: Extracellular fructosyltransferase (FTase, E.C.2.4.1.9) from Aspergillus oryzaeIPT-301 was immobilized on silica gel by adsorption and biochemically characterized aiming at its application in the transfructosylation reaction of sucrose for the production of fructooligossaccarides (FOS). RESULTS: The transfructosylation activity (AT) was maximized by the experimental design in function of the reaction pHs and temperatures. The AT of the immobilized enzyme showed the kinetics behavior described by the Hill model. The immobilized FTase showed reuse capacity for six consecutive reaction cycles and higher pH and thermal stability than the soluble enzyme. CONCLUSION: These results suggest a high potential of application of silica gel as support for FTase immobilization aiming at FOS production.
Entities:
Keywords:
Aspergillus; Enzymatic characterization; Fructosyltransferase; Immobilization; Silica gel
Authors: Natália B Machado; João P Miguez; Iara C A Bolina; Adriana B Salviano; Raphael A B Gomes; Olga L Tavano; Jaine H H Luiz; Paulo W Tardioli; Érika C Cren; Adriano A Mendes Journal: Enzyme Microb Technol Date: 2019-05-03 Impact factor: 3.493