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KMID : 0545120180280091447
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Journal of Microbiology and Biotechnology
2018 Volume.28 No. 9 p.1447 ~ p.1456
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Sustainable Production of Dihydroxybenzene Glucosides Using Immobilized Amylosucrase from Deinococcus geothermalis
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Lee Hun-Sang
Kim Tae-Su
Parajuli Prakash
Pandey Ramesh Prasad
Sohng Jae-Kyung
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Abstract
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The amylosucrase encoding gene from Deinococcus geothermalis DSM 11300 (DgAS) was codonoptimized and expressed in Escherichia coli. The enzyme was employed for biosynthesis of three different dihydroxybenzene glucosides using sucrose as the source of glucose moiety. The reaction parameters, including temperature, pH, and donor (sucrose) and acceptor substrate concentrations, were optimized to increase the production yield. This study demonstrates the highest ever reported molar yield of hydroquinone glucosides 325.6 mM (88.6 g/l), resorcinol glucosides 130.2 mM (35.4 g/l) and catechol glucosides 284.4 mM (77.4 g/l) when 400 mM hydroquinone, 200 mM resorcinol and 300 mM catechol, respectively, were used as an acceptor substrate. Furthermore, the use of commercially available amyloglucosidase at the end of the transglycosylation reaction minimized the glucooligosaccharides, thereby enhancing the target productivity of mono-glucosides. Moreover, the immobilized DgAS on Amicogen LKZ118 beads led to a 278.4 mM (75.8 g/l), 108.8 mM (29.6 g/l) and 211.2 mM (57.5 g/l) final concentration of mono-glycosylated product of hydroquinone, catechol and resorcinol at 35 cycles, respectively, when the same substrate concentration was used as mentioned above. The percent yield of the total glycosides of hydroquinone and catechol varied from 85% to 90% during 35 cycles of reactions in an immobilized system, however, in case of resorcinol the yield was in between 65% to 70%. The immobilized DgAS enhanced the efficiency of the glycosylation reaction and is therefore considered effective for industrial application.
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KEYWORD
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Dihyroxybenzene glucosides, amylosucrase, amyloglucosidase, deinococcus geothermalis, enzyme Immobilization
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