Glycosylation of Ganoderic Acid G by Bacillus Glycosyltransferases

Wu, Jiumn-Yih; Ding, Hsiou-Yu; Wang, Tzi‐Yuan; Zhang, Yun-Rong; Chang, Te‐Sheng

doi:10.3390/ijms22189744

Cited by 4 publications

(4 citation statements)

References 24 publications

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“…The previous study showed that BsGT110 could glycosylate the C-26 carboxyl groups of GAA [7] and GAG [8]. Thus, to produce rare Ganoderma saponins, the enzyme was evaluated for its glycosylation activity toward another Ganoderma triterpenoid, GAF (Figure 1).…”

Section: Bsgt110 Biotransforming Gafmentioning

confidence: 99%

“…The results showed that the aqueous solubility and stability of the isoflavone glucosides (8-OHDe-7-O-β-glucoside and 8-OHDe-8-O-β-glucoside) were greatly improved. Moreover, BsGT110 was recently demonstrated to glycosylate both ganoderic acid A (GAA) and ganoderic acid G (GAG), two Ganoderma triterpenoids, to produce two novel Ganoderma saponins, GAA-26-O-β-glucoside [7] and GAG-26-O-β-glucoside [8], respectively. In fact, BsGT110 was the first identified GT catalyzing the glycosylation of a triterpenoid at the C-26 position.…”

Section: Introductionmentioning

confidence: 99%

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Glycosylation of Ganoderic Acid F by Bacillus Glycosyltransferase

Chang

2022

Agrochemicals

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Ganoderma lucidum is a medicinal fungus and has been used for improvements of health or prevention of certain diseases in Asia for thousands of years. Despite numerous kinds of triterpenoids having been identified from G. lucidum, few natural Ganoderma triterpenoids exist in the form of glycosides (saponins). To expand the diversity of Ganoderma triterpenoids and find rare Ganoderma saponins, ganoderic acid F (GAF), a Ganoderma triterpenoid, was biotransformed by a glycosyltransferase (BsGT110) from Bacillus subtilis ATCC (American type culture collection) 6633. The results showed that BsGT110 catalyzed biotransformation of GAF to produce a metabolite, which was confirmed as a GAF glucoside by mass–mass spectroscopy. The GAF glucoside showed 89-fold higher aqueous solubility than that of GAF. The present study highlights the utility of BsGT110 in the production of novel Ganoderma triterpenoid saponins, and the newly identified and highly soluble GAF glucoside can be studied for its bioactivity in the future.

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Section: Bsgt110 Biotransforming Gafmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Glycosylation of Ganoderic Acid F by Bacillus Glycosyltransferase

Chang

2022

Agrochemicals

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“…In spite of the diversity of Ganoderma triterpenoids, only a few Ganoderma triterpenoid saponins were identified [ 7 , 8 , 9 ]. In previous studies, we found that several bacterial GTs are able to glycosylate Ganoderma triterpenoids to Ganoderma triterpenoid glycosides [ 10 , 11 , 12 , 13 ]. These discovered glycosides were all β -linkage aglycons.…”

Section: Introductionmentioning

confidence: 99%

Novel Glycosylation by Amylosucrase to Produce Glycoside Anomers

Ding

Luo

et al. 2022

Biology

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Glycosylation occurring at either lipids, proteins, or sugars plays important roles in many biological systems. In nature, enzymatic glycosylation is the formation of a glycosidic bond between the anomeric carbon of the donor sugar and the functional group of the sugar acceptor. This study found novel glycoside anomers without an anomeric carbon linkage of the sugar donor. A glycoside hydrolase (GH) enzyme, amylosucrase from Deinococcus geothermalis (DgAS), was evaluated to glycosylate ganoderic acid F (GAF), a lanostane triterpenoid from medicinal fungus Ganoderma lucidum, at different pH levels. The results showed that GAF was glycosylated by DgAS at acidic conditions pH 5 and pH 6, whereas the activity dramatically decreased to be undetectable at pH 7 or pH 8. The biotransformation product was purified by preparative high-performance liquid chromatography and identified as unusual α-glucosyl-(2→26)-GAF and β-glucosyl-(2→26)-GAF anomers by mass and nucleic magnetic resonance (NMR) spectroscopy. We further used DgAS to catalyze another six triterpenoids. Under the acidic conditions, two of six compounds, ganoderic acid A (GAA) and ganoderic acid G (GAG), could be converted to α–glucosyl-(2→26)-GAA and β–glucosyl-(2→26)-GAA anomers and α-glucosyl-(2→26)-GAG and β-glucosyl-(2→26)-GAG anomers, respectively. The glycosylation of triterpenoid aglycones was first confirmed to be converted via a GH enzyme, DgAS. The novel enzymatic glycosylation-formed glycoside anomers opens a new bioreaction in the pharmaceutical industry and in the biotechnology sector.

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“…For instance, four glycosyltransferases (GTs) from Bacillus sp., including BtGT_16345 from the B. thuringiensis GA A07 strain and three GTs (BsGT110, BsUGT398, and BsUGT489) from the B. subtilis ATCC 6633 strain were used to biotransform ganoderic acid G (GAG), a saponin from Ganoderma lucidum. BsUGT489 and BsGT110 successfully glycosylated GAG into GAG-3-O-β-glucoside and GAG-26-O-β-glucoside, which showed 54-fold and 97-fold higher aqueous solubilities, respectively, compared to GAG [11]. Enzymatic methods have also been used for the production of tentative metabolites of bioactive compounds.…”

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confidence: 99%