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Geise Camila de Araujo Ribeiro,Pedro Fernandes,Dayse Alessandra Almeida Silva,Hugo Neves Brandao,Sandra Aparecida de Assis 한국식품과학회 2021 Food Science and Biotechnology Vol.30 No.7
The crude extract containing inulinase fromRhodotorula mucilaginosa was obtained by submergedfermentation. Inulinase was immobilized on chicken eggshellby physical adsorption and covalent crosslinking,using glutaraldehyde as a crosslinking reagent, and Celiteby adsorption. Fructooligosaccharides production wasperformed using immobilized inulinase (5%, w/v) andinulin substrate solution under experimental conditionsevaluated through Doehlert experimental design. The productionof inulinase was optimized for concentrations ofD-glucose and yeast extract at 12.5 and 0.5 g/L, respectively,resulting in an optimal activity of 0.62 U. Theoptimal pH and temperature for enzyme activity were 8.0and 75 C, respectively, leading to an optimal activity of3.54 U. The highest immobilization efficiency (46.27%)was obtained upon immobilization on Celite. Immobilizationby adsorption to eggshell allowed for specific activityof 4.15 U/g, and adsorption to Celite resulted in specificactivity of 3.70 U/g. The highest titer in fructooligosaccharideswas obtained with an initial inulin concentrationof 250 g/L (25%, w/v), and a reaction time of 16 h. Hence,immobilized inulinase proved to be a promising catalyst forfructooligosaccharides production since the formulation isperformed through a simple, low-cost, and large-scaleapplicable methodology.