Production of Hesperetin Using a Covalently Multipoint Immobilized Diglycosidase from Acremonium sp. DSM24697

PIÑUEL, L.; BRECCIA J.D.; GUISÁN JM; LÓPEZ-GALLEGO F.

JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY

KARGER

Lugar: Basel; Año: 2013 p. 410 - 417

1464-1801

The diglycosidase α-rhamnosyl-β-glucosidase (EC 3.2.1.168)from the fungus Acremonium sp. DSM24697 was immobilizedon several agarose-based supports. Covalent multipointimmobilization onto glyoxyl-activated agarose was selectedas the more stable preparation at high concentrationof dimethyl sulfoxide (DMSO) and high temperature. The optimalconditions for the immobilization process involved anincubation of the enzyme with agarose beads containing220 μmol of glyoxyl groups per gram at pH 10 and 25 ° C for24 h. The hydrolysis of hesperidin carried out in 10% v/vDMSO at 60 ° C for 2 h reached 64.6% substrate conversionand a specific productivity of 2.40 mmol h ?1 g ?1 . Under theseconditions, the process was performed reutilizing the catalystfor up to 18 cycles, maintaining >80% of the initial activityand a constant productivity 2.96 ± 0.42 μmol ?1 h ?1 g ?1 . Tothe best of our knowledge, such productivity is the highestachieved for hesperetin production through an enzymaticapproach.