earticle

영어

Dihydroxybenzenes exhibit biological functions such as anti- cancer, anti- inflammation, and antioxidants. They are also widely used in the cosmetics industry and as a treatment of skin related disease. In spite of these functions, they are easily oxidized by light in aqueous solutions and are limited by toxicity and side effects. The transglycosylation for these compounds have been shown to resolve these problems of solubility, stability and toxicity. Amylosucrase from Deinococcus geothermalis (DGAS) has been selected as the enzyme to be used for the transglycosylation. This enzyme is industrially useful because it supplies glucose using a relatively inexpensive donor substrate (sucrose). In this study, amylosucrase gene ( dgas) was codon optimized according to E. coli BL21 (DE3) codon usage. Sucrose was used as a source of glucose and it was used to produce three dihydroxybenzene (Hydroquinone, Resorcinol, Catechol) glucosides derivatives. Optimization of temperature, pH, donor (sucrose) and acceptor substrates concentrations increased glucoside derivative productivity. In addition, amyloglucosidase was used to reduced gluco-oligosaccharides and increased the production of mono-glucoside derivatives. Finally, the DgAS enzyme was immobilized on AMICOGEN LKZ118 beads. Immobilized enzyme could be used repeatedly up to 35 ~ 40 cycle on average. The percent yield of the total glycosides of hydroquinone and catechol varied from 85% to 90% until in immobilized system, however, in case of resorcinol the yield was in between 65% to 70%. It showed production of hydroquinone-mono-glucoside 13.3 g (35 cycle, 175mL), resorcinol-mono- glucoside 5.9 g ( 40 cycle, 200mL) and catechol-mono- glucoside 11.5g ( 40 cycle, 200mL) using a immobilized enzyme. The immobilized DgAS 1s cost reduction due to the separation and repeated use of the enzyme, to be effective for industrial application.