Innovative Immobilization of Aspergillus aculeatus OI4C2 Fructosyltransferase on MANAE-Agarose Cross-Linked with Genipin for Enhanced Production of Fructooligosaccharides

TL;DR

This study shows that immobilizing an enzyme from Aspergillus aculeatus on a genipin-cross-linked agarose matrix improves its efficiency and stability for producing fructooligosaccharides.

Contribution

The novel use of genipin-cross-linked MANAE-agarose for immobilizing A. aculeatus FTase enhances FOS production and enzyme stability.

Findings

Immobilized FTase achieved 97.37 g L–1 FOS, higher than 73.44 g L–1 from the free enzyme.

The immobilized enzyme retained 50% activity after 12 reuse cycles.

It showed improved thermal and acidic pH stability compared to the free enzyme.

Abstract

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.

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