Properties of fructosyltransferase from Aureobasidium pullulans immobilized on an acrylic carrier

Abstract

Optimization of immobilization conditions was carried out for covalent binding of Aureobasidium pullulans fructosyltransferase to a copolymer of butyl acrylate and ethylene glycol dimethacrylate using a glutaraldehyde method. It was found that the highest activity of the preparation could be obtained for the immobilization pH 6.0 and initial protein amount 8.5 g per dm3 of the carrier. Effects of the reaction pH, temperature, and initial sucrose concentration on the activity and stability of the preparation were analyzed. Further investigations involved storage stability and operational stability in a mechanically stirred-tank reactor.

Enhancement of fructosyltransferase stability by immobilization on polyhydroxybutyrate and glutaraldehyde‐activated polyhydroxybutyrate for fructooligosaccharides production

“…immobilized onto niobium ore showed high activity and good stability at pH from 4.5 to 6.0 6 . Similarly, the FTase from Aureobasidium pullulans CCY 27–1‐94 immobilized on an acrylic carrier showed relative activity higher than 85% at pH values from 3 to 6 after 1 h of incubation 67 …”

“…5). Specifically, pH inactivation of enzymes involves the unfolding of the protein molecule due to changes in the electrostatic balance and hydrogen bonds that increase due to a pH‐induced change of the ionization state of the enzyme ionogenic group 67 . It was reported that the FTase from A. oryzae IPT‐301 immobilized by adsorption on silica gel showed high stability at pH values from 5.0 to 6.5, with relative activity higher than 95% 7 .…”

“…6 Similarly, the FTase from Aureobasidium pullulans CCY 27-1-94 immobilized on an acrylic carrier showed relative activity higher than 85% at pH values from 3 to 6 after 1 h of incubation. 67 Storage stability of the immobilized enzymes The storage stability of the immobilized FTase is shown in Fig. 6.…”

Parameters Affecting the Performance of Immobilized Enzyme

“…So far, various carriers and methodologies have been used for enzyme immobilization in order to improve the properties of free enzyme [8][9][10][11]. In fact, the performance of immobilized lipase relies on several important factors including immobilization methods, immobilization carrier materials, enzyme pretreatment before immobilization, and enzyme loading on the carriers.…”