NDLI: Pinoresinol diglucoside is screened as a putative α-glucosidase inhibiting compound in Actinidia arguta leaves

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Pinoresinol diglucoside is screened as a putative α-glucosidase inhibiting compound in Actinidia arguta leaves

Content Provider	Semantic Scholar
Author	Kwon, Dodan Kim, Gyoung Deuck Kang, Wonseok Park, Jeong-Eun Kim, Song Hee Choe, Eunok Kim, Jung-In Auh, Joong-Hyuck
Copyright Year	2014
Abstract	Actinidia arguta leaves are consumed as a popular food material in Korea and have been reported to exert beneficial effects on humans due to its constituent polyphenolic compounds. In this study, the α-glucosidase inhibitory compounds in A. arguta were screened and identified through α-glucosidase-guided fractionation and metabolomic analysis. The 50% ethanol extracts of A. arguta showed strong inhibitory effect (32.6%), which was comparable to acarbose as a positive control (30.0%). Through multiple steps of fractionation, pinoresinol diglucoside and fertaric acid were identified as the major potent compounds in A. arguta inhibiting α-glucosidase activity by liquid chromatography mass spectrometry analysis and metabolomic comparison. Particularly, because pinoresinol and its glycosides have been demonstrated as α-glucosidase inhibitory agents, pinoresinol diglucoside was proposed to be a putative key compound for α-glucosidase inhibition in A. arguta. This is the first study demonstrating the anti-diabetic effect of a pinoresinol-containing fraction of A. arguta and would be useful for its application as a natural α-glucosidase inhibitor.
Starting Page	473
Ending Page	479
Page Count	7
File Format	PDF HTM / HTML
DOI	10.1007/s13765-014-4167-0
Volume Number	57
Alternate Webpage(s)	https://applbiolchem.springeropen.com/track/pdf/10.1007/s13765-014-4167-0
Alternate Webpage(s)	https://applbiolchem.springeropen.com/track/pdf/10.1007/s13765-014-4575-1
Alternate Webpage(s)	https://doi.org/10.1007/s13765-014-4167-0
Journal	Journal of the Korean Society for Applied Biological Chemistry
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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