Biochemical characterization of extracellular fructosyltransferase from Aspergillus oryzae IPT-301 immobilized on silica
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ORIGINAL RESEARCH PAPER
Biochemical characterization of extracellular fructosyltransferase from Aspergillus oryzae IPT-301 immobilized on silica gel for the production of fructooligosaccharides Larissa Lemos Faria . Sergio Andres Villalba Morales . Jose´ Pedro Zanetti Prado . Giancarlo de Souza Dias . Alex Fernando de Almeida . Michelle da Cunha Abreu Xavier Elda Sabino da Silva . Alfredo Eduardo Maiorano . Rafael Firmani Perna
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Received: 27 July 2020 / Accepted: 29 September 2020 Ó Springer Nature B.V. 2020
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. Keywords Fructosyltransferase Aspergillus Immobilization Silica gel Enzymatic characterization
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s10529-020-03016-7) contains supplementary material, which is available to authorized users. L. L. Faria S. A. V. Morales J. P. Z. Prado G. S. Dias R. F. Perna (&) Institute of Science and Technology, Federal University of Alfenas (UNIFAL-MG), Jose´ Aure´lio Vilela Road 11999, Km 533, Poc¸os de Caldas, MG Zip Code 37715-400, Brazil e-mail: [email protected] A. F. de Almeida M. C. A. Xavier Department of Bioprocess Engineering and Biotechnology, Federal University of Tocantins (UFT), Badejos Street 69-72, Jardim Cervilha, Gurupi, TO Zip Code 77404-970, Brazil E. S. da Silva A. E. Maiorano Bionanomanufacturing Center, Institute for Technological Research (IPT-SP), Av. Prof. Almeida Prado 532, University City, Sa˜o Paulo, SP Zip Code 05508-901, Brazil
Introduction Fructosyltransferase (FTase, E.C.2.4.1.9) is an enzyme that catalyzes the transference of fructosyl groups to sucrose, via b-2,1 glycosidic bonds, for the production of fructooligossaccarides (FOS), fructose oligomers with high commercial interest in food and pharmaceutical industries (Yun and Song 1996; Huang et al. 2016; Castro et al. 2017; Nobre et al. 2018). Short-chain FOS such as 1-kestose (GF2), nystose (GF3) and b-fructofuranosylnystose (GF4) are important functional sugars in food fabrication because their consumption offers several benefits to human health, such as: low-calorie, prebiotic and anticariogenic properties, help in the control of
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