INVESTIGADORES
BRECCIA Javier Dario
artículos
Título:
PRODUCCION OF HESPERETIN USING A COVALENTLY MULTIPOINT IMMOBILIZED DIGLYCOSIDASE FROM Acremonium sp. DSM24697
Autor/es:
PINUEL L; BRECCIA JD; GUISÁN JM; LOPEZ GALLEGO F
Revista:
JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY
Editorial:
KARGER
Referencias:
Año: 2013 vol. 23 p. 410 - 417
ISSN:
1464-1801
Resumen:
The diglycosidase -rhamnosyl--glucosidase (EC 3.2.1.168) from the fungus Acremonium sp. DSM24697 was immobilized on several agarose based supports. Covalent multipoint immobilization onto glyoxyl activated agarose was selected as the more stable preparation at high concentration of DMSO and temperature. The optimal conditions for the immobilization process involved an incubation of the enzyme with agarose beads containing 220 mol of glyoxyl groups per gram at pH 10, 25°C for 24 h. The hydrolysis of hesperidin carried out in 10%v/v DMSO at 60°C for 2 h reached 64.6% substrate conversion and a specific productivity of 2.40 mmol h-1 g-1. Under these conditions, the process was performed reutilizing the catalyst up to 18 cycles maintaining > 80% of the initial activity and a constant productivity 2.96 ± 0.42 µmol-1 h-1 g-1. To the best of our knowledge, such productivity is the highest achieved for hesperetin production throughout an enzymatic approach.