Snailase: A Promising Tool for the Enzymatic Hydrolysis of Flavonoid Glycosides From Plant Extracts
Plants typically contain a broad spectrum of flavonoids in varying concentrations. As a rule, several flavonoid classes occur in parallel, and, even for a single flavonoid, divergent glycosylation patterns are frequently observed, many of which are not commercially available. This can be challenging...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-06-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fpls.2022.889184/full |
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| author | Christoph Kornpointner Jakob Scheibelreiter Heidi Halbwirth |
| author_facet | Christoph Kornpointner Jakob Scheibelreiter Heidi Halbwirth |
| author_sort | Christoph Kornpointner |
| collection | DOAJ |
| description | Plants typically contain a broad spectrum of flavonoids in varying concentrations. As a rule, several flavonoid classes occur in parallel, and, even for a single flavonoid, divergent glycosylation patterns are frequently observed, many of which are not commercially available. This can be challenging in studies in which the distribution between flavonoid classes, or features that are not affected by glycosylation patterns, are adressed. In addition, hydrolysis simplifies the quantification process by reducing peak interferences and improving the peak intensity due to the accumulation of the respective aglycone. Effective removal of glycose moieties can also be relevant for technological applications of flavonoid aglycones. Herein, we present a fast and reliable method for the enzymatic hydrolysis glycosides from plant extracts using the commercial enzyme mix snailase, which provided the highest aglycone yields across all investigated flavonoids (aurones: leptosidin, maritimetin, sulfuretin; chalcones: butein, lanceoletin, okanin, phloretin; dihydroflavonols: dihydrokaempferol; flavanones: eriodictyol, hesperetin; flavones: acacetin, apigenin, diosmetin, luteolin; flavonols: isorhamnetin, kaempferol, myricetin, quercetin; isoflavones: biochanin A, formononetin, genistein) from methanolic extracts of nine plants (Bidens ferulifolia, Coreopsis grandiflora, Fagus sylvatica, Malus × domestica, Mentha × piperita, Petunia × hybrida, Quercus robur, Robinia pseudoacacia, and Trifolium pratense) in comparison to four other enzymes (cellobiase, cellulase, β-glucosidase, and pectinase), as well as to acidic hydrolysis by hydrochloric acid. |
| first_indexed | 2024-04-13T20:37:06Z |
| format | Article |
| id | doaj.art-7e040ded0d694a6ba54d3e8de4663fa6 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-04-13T20:37:06Z |
| publishDate | 2022-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-7e040ded0d694a6ba54d3e8de4663fa62022-12-22T02:31:00ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2022-06-011310.3389/fpls.2022.889184889184Snailase: A Promising Tool for the Enzymatic Hydrolysis of Flavonoid Glycosides From Plant ExtractsChristoph KornpointnerJakob ScheibelreiterHeidi HalbwirthPlants typically contain a broad spectrum of flavonoids in varying concentrations. As a rule, several flavonoid classes occur in parallel, and, even for a single flavonoid, divergent glycosylation patterns are frequently observed, many of which are not commercially available. This can be challenging in studies in which the distribution between flavonoid classes, or features that are not affected by glycosylation patterns, are adressed. In addition, hydrolysis simplifies the quantification process by reducing peak interferences and improving the peak intensity due to the accumulation of the respective aglycone. Effective removal of glycose moieties can also be relevant for technological applications of flavonoid aglycones. Herein, we present a fast and reliable method for the enzymatic hydrolysis glycosides from plant extracts using the commercial enzyme mix snailase, which provided the highest aglycone yields across all investigated flavonoids (aurones: leptosidin, maritimetin, sulfuretin; chalcones: butein, lanceoletin, okanin, phloretin; dihydroflavonols: dihydrokaempferol; flavanones: eriodictyol, hesperetin; flavones: acacetin, apigenin, diosmetin, luteolin; flavonols: isorhamnetin, kaempferol, myricetin, quercetin; isoflavones: biochanin A, formononetin, genistein) from methanolic extracts of nine plants (Bidens ferulifolia, Coreopsis grandiflora, Fagus sylvatica, Malus × domestica, Mentha × piperita, Petunia × hybrida, Quercus robur, Robinia pseudoacacia, and Trifolium pratense) in comparison to four other enzymes (cellobiase, cellulase, β-glucosidase, and pectinase), as well as to acidic hydrolysis by hydrochloric acid.https://www.frontiersin.org/articles/10.3389/fpls.2022.889184/fullsnailaseenzymatic hydrolysisflavonoid aglyconesacidic hydrolysisflavonoidsanthochlors |
| spellingShingle | Christoph Kornpointner Jakob Scheibelreiter Heidi Halbwirth Snailase: A Promising Tool for the Enzymatic Hydrolysis of Flavonoid Glycosides From Plant Extracts Frontiers in Plant Science snailase enzymatic hydrolysis flavonoid aglycones acidic hydrolysis flavonoids anthochlors |
| title | Snailase: A Promising Tool for the Enzymatic Hydrolysis of Flavonoid Glycosides From Plant Extracts |
| title_full | Snailase: A Promising Tool for the Enzymatic Hydrolysis of Flavonoid Glycosides From Plant Extracts |
| title_fullStr | Snailase: A Promising Tool for the Enzymatic Hydrolysis of Flavonoid Glycosides From Plant Extracts |
| title_full_unstemmed | Snailase: A Promising Tool for the Enzymatic Hydrolysis of Flavonoid Glycosides From Plant Extracts |
| title_short | Snailase: A Promising Tool for the Enzymatic Hydrolysis of Flavonoid Glycosides From Plant Extracts |
| title_sort | snailase a promising tool for the enzymatic hydrolysis of flavonoid glycosides from plant extracts |
| topic | snailase enzymatic hydrolysis flavonoid aglycones acidic hydrolysis flavonoids anthochlors |
| url | https://www.frontiersin.org/articles/10.3389/fpls.2022.889184/full |
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