Authors: Carceller, JM; Galan, JPM; Monti, R; Bassan, JC; Filice, M; Yu, JH; Climent, MJ; Iborra, S; Corma, A

Article; Early Access.
ChemCatChem. vol: . page: 1867-3880.
Date: . .
Doi: 10.1002/cctc.202000320.

The crude naringinase from Penicillium decumbens and a purified naringinase with high alpha-L-rhamnosidase activity could be covalently immobilized on two-dimensional zeolite ITQ-2 after surface modification with glutaraldehyde. The influence of pH and temperature on the enzyme activity (in free and immobilized forms) as well as the thermal stability were determined using the specific substrate: p-nitrophenyl-alpha-L-rhamnopyranoside (Rha-pNP). The crude and purified naringinase supported on ITQ-2 were applied in the hydrolysis of naringin, giving the flavonoids naringenin and prunin respectively with a conversion >90 % and excellent selectivity. The supported enzymes showed long term stability, being possible to perform up to 25 consecutive cycles without loss of activity, showing its high potential to produce the valuable citrus flavonoids prunin and naringenin. We have also succeeded in the application of the immobilized crude naringinase on ITQ-2 for debittering grapefruit juices in a continuous process that was maintained operating for 300 h, with excellent results..