Effective production of lactosucrose using β‐fructofuranosidase and glucose oxidase co‐immobilized by sol–gel encapsulation

Abstract

The production of lactosucrose is hampered by the costly use of β‐fructofuranosidase, which shows poor stability and a low efficiency in transfructosylation activity. Immobilization could improve enzyme stability and realize the cyclic utilization at a reduced cost. In order to eliminate the by‐product inhibition and improve the transfructosylation efficiency, β‐fructofuranosidase and glucose oxidase were co‐immobilized by sol–gel encapsulation and the subsequent production efficiency of lactosucrose was investigated. The as‐prepared immobilized bi‐enzymes retained 85.39% of their initial activity at an enzyme concentration of 1.47 mg/g·sol during immobilization and showed great operational stability (maintaining 78.5% of their initial activity) after 15 consecutive reuses. The yield of lactosucrose synthesized by immobilized bi‐enzymes reached 160.8 g/L under the optimized conditions, which was relatively higher than previous reported results. Moreover, the yield of lactosucrose synthesized by immobilized bi‐enzymes was significantly improved as compared to that synthesized by immobilized β‐fructofuranosidase. HPLC and NMR spectrum results confirmed the presence of lactosucrose during immobilized bi‐enzymes catalysis. Furthermore, a relatively high purity of lactosucrose was obtained (87.4% determined by HPLC) after separation with Diaion UBK535 calcium ester resin, and the optimal conditions for separation of lactosucrose were investigated. These results indicated that the co‐immobilization of β‐fructofuranosidase‐glucose oxidase was helpful to improve the production of lactosucrose with low costs, which can be used in continuous lactosucrose production in food industry in advantages of high stability and reusability. And the as‐prepared lactosucrose with high purity can be applied to many kinds of food as functional additives.

Biocatalytic synthesis of lactosucrose using a recombinant thermostable β-fructofuranosidase from Arthrobacter sp. 10138

“…We speculated that there may be product or glucose inhibition. Recently, enzyme immobilization [33] and glucose oxidase addition [34] have been used for the continuous lactosucrose production with higher productivity. These techniques may increase the industrialization feasibility of lactosucrose biosynthesis.…”

Multicatalytic Hybrid Materials for Biocatalytic and Chemoenzymatic Cascades—Strategies for Multicatalyst (Enzyme) Co-Immobilization

“…However, no study was carried out integrating the oxidation of HMF to DFF, by free GOaseM 3-5 and HRP, and oxidation of DFF to FDCA, with the immobilized PaoABC and catalase. Other examples of applications of enzymatic co-immobilization by gel encapsulation are given by studies of Long and co-workers [81,82] on the production of lactosucrose. Sankar et al [71] co-immobilized laccase, cellulose, and β-glucosidase for the pretreatment Other examples of applications of enzymatic co-immobilization by gel encapsulation are given by studies of Long and co-workers [81,82] on the production of lactosucrose.…”

“…Other examples of applications of enzymatic co-immobilization by gel encapsulation are given by studies of Long and co-workers [81,82] on the production of lactosucrose. Sankar et al [71] co-immobilized laccase, cellulose, and β-glucosidase for the pretreatment Other examples of applications of enzymatic co-immobilization by gel encapsulation are given by studies of Long and co-workers [81,82] on the production of lactosucrose. Sankar et al [71] co-immobilized laccase, cellulose, and β-glucosidase for the pretreatment of lignocellulosic biomass.…”

Recent Advances of Macromolecular Hydrogels for Enzyme Immobilization in the Food Products

“…It has many uses; for example, it scavenges oxygen in the food industry effectively, catalyzes the reaction of glucose and oxygen that generates glucuronic acid, and successfully removes oxygen from food and beverages to prolong their shelf life. 31 , 32 …”