Efficient enzymatic modification of epigallocatechin gallate in ionic liquids
Epigallocatechin gallate (EGCG), the main polyphenolic substance in tea, exhibits well-known biological benefits. In order to improve fat solubility and bioavailability, a novel path for the lipase enzymatic transesterification synthesis of acylated EGCG derivatives in an ionic liquid solvent was es...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2021-04-01
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| Series: | Green Chemistry Letters and Reviews |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/17518253.2021.1926549 |
| _version_ | 1819105651275595776 |
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| author | Song Zhu Na Meng Yue Li Shang-Wei Chen |
| author_facet | Song Zhu Na Meng Yue Li Shang-Wei Chen |
| author_sort | Song Zhu |
| collection | DOAJ |
| description | Epigallocatechin gallate (EGCG), the main polyphenolic substance in tea, exhibits well-known biological benefits. In order to improve fat solubility and bioavailability, a novel path for the lipase enzymatic transesterification synthesis of acylated EGCG derivatives in an ionic liquid solvent was established. The optimal reaction parameters were determined and a maximum conversion of the transesterification reaction was achieved at 98.65%. [Bmim][BF4] was the best reaction medium and the immobilized lipase Novozym 435 was the best catalyst. The enzyme was added to a final concentration of 2% (w/w, EGCG), and the reaction was performed at an optimum temperature of 70°C stirring for 10 h at 250 rpm. The most suitable acyl donor, vinyl acetate, and EGCG were mixed at a molar ratio of 90:1 for the reaction. The structure of the purified acetylated EGCG was determined to be 5″-O-acetyl-EGCG and 3″, 5″-2-O-acetyl-EGCG by mass spectrometry, NMR, and infrared analyses. |
| first_indexed | 2024-12-22T02:25:38Z |
| format | Article |
| id | doaj.art-b63528ec88eb4564a480257f2e0062ee |
| institution | Directory Open Access Journal |
| issn | 1751-8253 1751-7192 |
| language | English |
| last_indexed | 2024-12-22T02:25:38Z |
| publishDate | 2021-04-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Green Chemistry Letters and Reviews |
| spelling | doaj.art-b63528ec88eb4564a480257f2e0062ee2022-12-21T18:42:01ZengTaylor & Francis GroupGreen Chemistry Letters and Reviews1751-82531751-71922021-04-0114241542410.1080/17518253.2021.19265491926549Efficient enzymatic modification of epigallocatechin gallate in ionic liquidsSong Zhu0Na Meng1Yue Li2Shang-Wei Chen3Jiangnan UniversityJiangnan UniversityJiangnan UniversityJiangnan UniversityEpigallocatechin gallate (EGCG), the main polyphenolic substance in tea, exhibits well-known biological benefits. In order to improve fat solubility and bioavailability, a novel path for the lipase enzymatic transesterification synthesis of acylated EGCG derivatives in an ionic liquid solvent was established. The optimal reaction parameters were determined and a maximum conversion of the transesterification reaction was achieved at 98.65%. [Bmim][BF4] was the best reaction medium and the immobilized lipase Novozym 435 was the best catalyst. The enzyme was added to a final concentration of 2% (w/w, EGCG), and the reaction was performed at an optimum temperature of 70°C stirring for 10 h at 250 rpm. The most suitable acyl donor, vinyl acetate, and EGCG were mixed at a molar ratio of 90:1 for the reaction. The structure of the purified acetylated EGCG was determined to be 5″-O-acetyl-EGCG and 3″, 5″-2-O-acetyl-EGCG by mass spectrometry, NMR, and infrared analyses.http://dx.doi.org/10.1080/17518253.2021.1926549egcg derivativesionic liquidsenzymaticimmobilized lipase |
| spellingShingle | Song Zhu Na Meng Yue Li Shang-Wei Chen Efficient enzymatic modification of epigallocatechin gallate in ionic liquids Green Chemistry Letters and Reviews egcg derivatives ionic liquids enzymatic immobilized lipase |
| title | Efficient enzymatic modification of epigallocatechin gallate in ionic liquids |
| title_full | Efficient enzymatic modification of epigallocatechin gallate in ionic liquids |
| title_fullStr | Efficient enzymatic modification of epigallocatechin gallate in ionic liquids |
| title_full_unstemmed | Efficient enzymatic modification of epigallocatechin gallate in ionic liquids |
| title_short | Efficient enzymatic modification of epigallocatechin gallate in ionic liquids |
| title_sort | efficient enzymatic modification of epigallocatechin gallate in ionic liquids |
| topic | egcg derivatives ionic liquids enzymatic immobilized lipase |
| url | http://dx.doi.org/10.1080/17518253.2021.1926549 |
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