Biosynthesis of sucrose-6-acetate catalyzed by surfactant-coated Candida rugosa lipase immobilized on sol-gel supports.

Sucrose-6-acetate is an important intermediate in the preparation of sucralose (a finest sweetener). In our study, Candida rugosa lipase coated with surfactant was firstly immobilized on sol-gel supports. Then, the immobilized enzyme was used in the regioselective synthesis of sucrose-6-acetate by transesterification of sucrose and vinyl acetate. The screening results revealed that Tween 80 was an ideal surfactant to coat lipase immobilized in sol-gel and exhibited the highest yield of sucrose-6-acetate. Other factors that influenced the yield during the preparation process were also studied. Under optimal conditions, the yield of sucrose-6-acetate could reach up to 78.68 %, while free lipase was easily inactivated in polar solvent. Thermal and operational stabilities were also improved significantly. Surfactant-coated lipase immobilized in sol-gel remained stable when the temperature was higher than 60 °C. Moreover, they could maintain high catalytic activity after six recycles. This strategy is economical, convenient and promising for the food industry.

Immobilization of lipase by dialdehyde cellulose crosslinked magnetic nanoparticles.

Cellulose microcrystalline (MCC) was widely used in pharmaceutical and chemical industries because of its low degree of polymerization and large specific surface area. As its modified form, dialdehyde cellulose (DAC) was used for cross-linking and immobilizing Rhizopus lipase together with magnetic nanoparticles (MNPs) due to its active aldehyde groups. In this study, in order to maintain the original enzyme activity as much as possible and improve the stability of lipase, the Rhizopus lipase was successfully immobilized on the magnetic dialdehyde cellulose nanoparticles (MDC). Specifically, the immobilization conditions including dosage of DAC, concentration of enzyme, immobilization time and temperature together with pH value of the reaction medium were optimized. Maximum immobilization yield (60.03 ± 0.49%) and recovery activity (88.88 ± 0.61%) can be obtained under the optimal process conditions. The changes in secondary structures of immobilized enzyme revealed the increment in conformational rigidity, which can be reflected in temperature and pH stability as well as tolerance of organic reagents. Additionally, the recovery activity of immobilized enzyme still reached 50.60 ± 0.59% after 30 d of storage and 52.10 ± 0.57% retained after 6 cycles. These results indicated the ideal application prospect of MDC in immobilized enzymes.