This study evaluated the use of genipin in monoamino-N-aminoethyl (MANAE)-agarose in the immobilization of fructosyltransferase (FTase) from Aspergillus aculeatus OI4C2, focusing on the stability and catalytic efficiency for the production of fructooligosaccharides (FOS) from sucrose. The immobilization of FTase on genipin-cross-linked MANAE-agarose achieved a 98.53% yield, 76.71% activity recovery, and 77.86% efficiency, and it resulted in the synthesis of predominantly short-chain fructooligosaccharides. Comparatively, the maximum amounts of FOS obtained were 73.44 g L-1 for the free enzyme and 97.37 g L-1 for the immobilized enzyme. Immobilization improved the thermal stability at 40-60 °C and increased the enzyme stability under acidic pH conditions (4.5-6.5) for up to 72 h. The operational stability of the immobilized enzyme retained 50% of its initial activity after 12 reuse cycles. These results indicate that A. aculeatus FTase immobilized on MANAE-agarose-genipin is a promising biocatalyst for large-scale FOS production, with prospects in the food, pharmaceutical, and nutraceutical industries.
Inagaki et al. (Mon,) studied this question.