Naringin

Not to be confused with Naringenin.
Naringin
Naringin
Naringin 3D
Names
IUPAC name
(2S)-4′,5-Dihydroxy-7-[α-L-rhamnopyranosyl-(1→2)-β-D-glucopyranosyloxy]flavan-4-one
Systematic IUPAC name
(2S)-7-{[(2S,3R,4S,5S,6R)-4,5-Dihydroxy-6-(hydroxymethyl)-3-{[(2S,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxy}oxan-2-yl]oxy}-5-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
Other names
Naringin
Naringoside
4′,5,7-Trihydroxyflavanone-7-rhamnoglucoside
Naringenin 7-O-neohesperidoside
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.030.502 Edit this at Wikidata
KEGG
UNII
  • InChI=1S/C27H32O14/c1-10-20(32)22(34)24(36)26(37-10)41-25-23(35)21(33)18(9-28)40-27(25)38-13-6-14(30)19-15(31)8-16(39-17(19)7-13)11-2-4-12(29)5-3-11/h2-7,10,16,18,20-30,32-36H,8-9H2,1H3/t10-,16+,18-,20+,21-,22+,23+,24-,25-,26-,27-/m1/s1 checkY
    Key: DFPMSGMNTNDNHN-CSIAVLANSA-N checkY
  • InChI=1/C27H32O14/c1-10-20(32)22(34)24(36)26(37-10)41-25-23(35)21(33)18(9-28)40-27(25)38-13-6-14(30)19-15(31)8-16(39-17(19)7-13)11-2-4-12(29)5-3-11/h2-7,10,16,18,20-30,32-36H,8-9H2,1H3/t10-,16+,18-,20+,21-,22+,23+,24-,25-,26-,27-/m1/s1
    Key: DFPMSGMNTNDNHN-CSIAVLANBN
  • O=C4c5c(O)cc(O[C@@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O[C@H]1O[C@@H]([C@H](O)[C@H](O)[C@H]1O)C)cc5O[C@H](c3ccc(O)cc3)C4
Properties
C27H32O14
Molar mass 580.54 g/mol
Melting point 166 °C (331 °F; 439 K)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
☒N verify (what is checkY☒N ?)

Naringin is a flavanone-7-O-glycoside between the flavanone naringenin and the disaccharide neohesperidose. The flavonoid naringin occurs naturally in citrus fruits, especially in grapefruit, where naringin is responsible for the fruit's bitter taste. In commercial grapefruit juice production, the enzyme naringinase can be used to remove the bitterness (debittering) created by naringin.[1] In humans naringin is metabolized to the aglycone naringenin (not bitter) by naringinase present in the gut.

  1. ^ Dicosimo R, McAuliffe J, Poulose AJ, Bohlmann G (2013). "Industrial use of immobilized enzymes". Chemical Society Reviews. 42 (15): 6437–6474. doi:10.1039/c3cs35506c. PMID 23436023.