An unusual chimeric amylosucrase generated by domain-swapping mutagenesis

Seo, Dong-Ho; Jung, Jong‐Hyun; Jung, Dong-Hyun; Park, Sunyoung; Yoo, Sang‐Ho; Kim, Young-Rok; Park, Cheon-Seok

doi:10.1016/j.enzmictec.2016.01.004

Cited by 31 publications

(24 citation statements)

References 61 publications

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“…The dgas gene has been described in previous studies [21,30]. This gene was identified in the genome of D. geothermalis DSM 11300.…”

Section: Expression and Activity Of Dgasmentioning

confidence: 88%

“…In contrast, IFAs were not detected in CE-SBE-DGAS ( Figure 5c and Table 2), indicating that IFAs in CE-SBE are successfully transglycosylated using DGAS. In previous studies, DGAS has been reported to transglycosylate a sugar moiety to the −OH group of the flavonoid aglycone [27,30,31]. It is also reported that glucose moiety was transferred to the isoflavone monoglucosides such as daidzin [36].…”

Section: Isoflavonementioning

confidence: 96%

“…In consideration of the stability of the IFAs, the temperature and pH for the DGAS-mediated transglycosylation of IFAs in this study were set at 45 • C and pH 5.0, respectively. in E. coli were investigated in the range of 30 to 55 °C and pH 4.0 to 9.0, respectively, based on a previous report of DGAS expression in E. coli [30]. It was previously reported that isoflavone glucosides can be thermally transformed to their corresponding aglycone forms during processing [34].…”

Section: Dgas Expression and Activitiesmentioning

confidence: 99%

“…Glycosylation reactions often involve a unimolecular (S N 1) or bimolecular (S N 2) nucleophilic substitution at the anomeric center [35]. in E. coli were investigated in the range of 30 to 55 °C and pH 4.0 to 9.0, respectively, based on a previous report of DGAS expression in E. coli [30]. It was previously reported that isoflavone glucosides can be thermally transformed to their corresponding aglycone forms during processing [34].…”

Section: Transglycosylation Of Ifas With Dgasmentioning

confidence: 99%

“…Amylosucrase (EC 2.4.1.4; AS) is a glycosyltransferase enzyme that belongs to the glucoside hydrolase family 13 [28]. One of the main characteristics of AS is that it catalyzes transglycosylation reactions to create α-1,4-glycosidic linkages given sucrose as a substrate [28,29]; AS promotes sucrose hydrolysis to release glucose and fructose, and α-1,4-oligosaccharides are formed using the released glucose as an acceptor [30]. Deinococcus geothermalis AS (DGAS) synthesizes α-1,4-glycosidic bonds using various acceptors such as flavonoids [31].…”

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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“…The dgas gene has been described in previous studies [21,30]. This gene was identified in the genome of D. geothermalis DSM 11300.…”

Section: Expression and Activity Of Dgasmentioning

confidence: 88%

Section: Isoflavonementioning

confidence: 96%

Section: Dgas Expression and Activitiesmentioning

confidence: 99%

Section: Transglycosylation Of Ifas With Dgasmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

Jung

Kim

et al. 2020

Molecules

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Identification and characterization of a novel high-activity amylosucrase from Salinispirillum sp. LH10-3-1

Gong

et al. 2023

Appl Microbiol Biotechnol

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Enzymatic modification of daidzin using heterologously expressed amylosucrase in Bacillus subtilis

Kim

Rha

Jung

et al. 2018

Food Sci Biotechnol

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Amylosucrases (ASase, EC 2.4.1.4) from Deinococcus geothermalis (DGAS) and Neisseria polysaccharea (NPAS) were heterologously expressed in Bacillus subtilis. While DGAS was successfully expressed, NPAS was not. Instead, NPAS was expressed in Escherichia coli. Recombinant DGAS and NPAS were purified using nickel-charged affinity chromatography and employed to modify daidzin to enhance its water solubility and bioavailability. Analyses by LC/MS revealed that the major products of transglycosylation using DGAS were daidzein diglucoside and daidzein triglucoside, whereas that obtained by NPAS was only daidzein diglucoside. The optimal bioconversion conditions for daidzein triglucoside, which was predicted to have the highest water-solubility among the daidzin derivatives, was determined to be 4% (w/v) sucrose and 250 mg/L daidzin in sodium phosphate pH 7.0, with a reaction time of 12 h. Taken together, we suggest that the yield and product specificity of isoflavone daidzin transglycosylation may be modulated by the source of ASase and reaction conditions.

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An unusual chimeric amylosucrase generated by domain-swapping mutagenesis

Cited by 31 publications

References 61 publications

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

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

Identification and characterization of a novel high-activity amylosucrase from Salinispirillum sp. LH10-3-1

Enzymatic modification of daidzin using heterologously expressed amylosucrase in Bacillus subtilis

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