High-efficiency enzymatic production of α-isoquercitrin glucosides by amylosucrase from Deinococcus geothermalis

Rha, Chan-Su; Choi, Jin Hyun; Jung, Young Sung; Kim, Eun-Ryoung; Ko, Minji; Seo, Dong-Ho; Kim, Dae‐Ok; Park, Cheon-Seok

doi:10.1016/j.enzmictec.2018.10.006

Cited by 29 publications

(42 citation statements)

References 40 publications

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“…Moreover, the transglycosylation of flavonoids using DGAS has been reported to occur primarily at the C-7 position of the A ring and at the C-4′ position of the B ring [27,32,36]. DGAS has been reported to attach four or fewer glucose moieties to flavonoids in transglycosylation [21,32]. Thus, we expected the total number of glucose moieties attached to IFAs in the DGAS transglycosylation process to be four.…”

Section: Transglycosylation Of Ifas With Dgasmentioning

confidence: 99%

“…Previous studies reported that recombinant AS created various stereostructures of acceptor compounds due to position-specific transglycosylation [27,33] (Figure 3). Moreover, the transglycosylation of flavonoids using DGAS has been reported to occur primarily at the C-7 position of the A ring and at the C-4′ position of the B ring [27,32,36]. DGAS has been reported to attach four or fewer glucose moieties to flavonoids in transglycosylation [21,32].…”

Section: Transglycosylation Of Ifas With Dgasmentioning

confidence: 99%

“…low resolution and greater difficultly separating them [32]. In addition, some isoquercitrin glucosides with high polarity have been reported to exist as isomers with the same number of sugars, the molecular weights of which were the same in mass spectra [32].…”

Section: Transglycosylation Of Ifas With Dgasmentioning

confidence: 99%

“…Deinococcus geothermalis AS (DGAS) synthesizes α-1,4-glycosidic bonds using various acceptors such as flavonoids [31]. DGAS enhances the water solubility of flavonoid aglycones by transglycosylation [21,31,32]. Compared with glycosyltransferase enzymes such as CGTase, DGAS can react with high substrate specificity using relatively inexpensive donors [27].…”

Section: Introductionmentioning

confidence: 99%

“…Compared with glycosyltransferase enzymes such as CGTase, DGAS can react with high substrate specificity using relatively inexpensive donors [27]. In addition, the interpretation of experimental results is easier when using DGAS because of fewer impurities and the limited number of transglycosylated sugar moieties [27,32,33]. These features of DGAS can be exploited to increase the solubility and bioavailability of bioactive phenolic compounds in soybeans.…”

Section: Introductionmentioning

confidence: 99%

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Enrichment of Polyglucosylated Isoflavones from Soybean Isoflavone Aglycones Using Optimized Amylosucrase Transglycosylation

Jung

Kim

et al. 2020

Molecules

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Isoflavones in soybeans are well-known phytoestrogens. Soy isoflavones present in conjugated forms are converted to aglycone forms during processing and storage. Isoflavone aglycones (IFAs) of soybeans in human diets have poor solubility in water, resulting in low bioavailability and bioactivity. Enzyme-mediated glycosylation is an efficient and environmentally friendly way to modify the physicochemical properties of soy IFAs. In this study, we determined the optimal reaction conditions for Deinococcus geothermalis amylosucrase-mediated α-1,4 glycosylation of IFA-rich soybean extract to improve the bioaccessibility of IFAs. The conversion yields of soy IFAs were in decreasing order as follows: genistein > daidzein > glycitein. An enzyme quantity of 5 U and donor:acceptor ratios of 1000:1 (glycitein) and 400:1 (daidzein and genistein) resulted in high conversion yield (average 95.7%). These optimal reaction conditions for transglycosylation can be used to obtain transglycosylated IFA-rich functional ingredients from soybeans.

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