Fructosyltransferase immobilized on a support based on TiO2: characterization, stability and its application.

VALDEÓN DH; ARAUJO, PZ; DAZ M; PEROTTI, NI

PROCESS BIOCHEMISTRY

ELSEVIER

Lugar: Amsterdam; Año: 2015

0032-9592

AbstractFructosyltransferase enzyme (Ftase) from Aureobasidium sp. ATCC 20524 was purified by two simple steps (ultrafiltration and precipitation) with a yield of 65% and purification factor of 16. Ftase was immobilized onto titanium dioxide (FTIO) and functionalized onto polyethyleneimine-TiO2 (FTIOP). FTIO and FTIOP showed an activity per gram of 903 and 9212, respectively. Optimum temperature was not change by immobilization. FTIO behavior did not present significant change in comparison with free enzyme. FTIOP kept maximum activity in a widely pH range regarding Ftase. The operational stability in both biocatalysts was above 80% in 7 working cycles, even more, FTIOP reached 98%. Gellan gum implementation, as encapsulated agent, enhance the design of the biocatalyst (FTIOPG) for technological due to the large size particle produced, this feature promote the elimination of the biocatalyst separation. Production of fructooligosaccharides from FTIOPG was about 60% for initial sucrose concentrations of 10%, 30% and 60%, results comparable to others.