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Conversion of Glycosylated Platycoside E to Deapiose-Xylosylated Platycodin D by Cytolase PCL5.


ABSTRACT: Platycosides, the saponins abundant in Platycodi radix (the root of Platycodon grandiflorum), have diverse pharmacological activities and have been used as food supplements. Since deglycosylated saponins exhibit higher biological activity than glycosylated saponins, efforts are on to enzymatically convert glycosylated platycosides to deglycosylated platycosides; however, the lack of diversity and specificities of these enzymes has limited the kinds of platycosides that can be deglycosylated. In the present study, we examined the enzymatic conversion of platycosides and showed that Cytolase PCL5 completely converted platycoside E and polygalacin D3 into deapiose-xylosylated platycodin D and deapiose-xylosylated polygalacin D, respectively, which were identified by LC-MS analysis. The platycoside substrates were hydrolyzed through the following novel hydrolytic pathways: platycoside E ? platycodin D3 ? platycodin D ? deapiosylated platycodin D ? deapiose-xylosylated platycodin D; and polygalacin D3 ? polygalacin D ? deapiosylated polygalacin D ? deapiose-xylosylated polygalacin D. Our results show that cytolast PCL5 may have a potential role in the development of biologically active platycosides that may be used for their diverse pharmacological activities.

SUBMITTER: Shin KC 

PROVIDER: S-EPMC7072768 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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Conversion of Glycosylated Platycoside E to Deapiose-Xylosylated Platycodin D by Cytolase PCL5.

Shin Kyung-Chul KC   Kim Dae Wook DW   Woo Hyun Sim HS   Oh Deok-Kun DK   Kim Yeong-Su YS  

International journal of molecular sciences 20200211 4


Platycosides, the saponins abundant in Platycodi radix (the root of <i>Platycodon</i> <i>grandiflorum</i>), have diverse pharmacological activities and have been used as food supplements. Since deglycosylated saponins exhibit higher biological activity than glycosylated saponins, efforts are on to enzymatically convert glycosylated platycosides to deglycosylated platycosides; however, the lack of diversity and specificities of these enzymes has limited the kinds of platycosides that can be degly  ...[more]

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