Lipase-catalyzed acylation of quercetin with cinnamic acid
Acylation of quercetin with cinnamic acid catalyzed by Candida antarctica lipase B (CAL-B) or Pseudomonas cepacia lipase C (PCL-C) was investigated. Specifically, the effects of reaction duration, incubation temperature, and molar ratio of substrates on bioconversion yield, initial rate of reaction,...
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| 格式: | 文件 |
| 语言: | English |
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Taylor & Francis
2016
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| 在线阅读: | http://psasir.upm.edu.my/id/eprint/54718/1/Lipase-catalyzed%20acylation%20of%20quercetin%20with%20cinnamic%20acid.pdf |
| _version_ | 1825931086566260736 |
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| author | Saik, Amy Yi Hsan Lim, Yau Yan Stanslas, Johnson Choo, Wee Sim |
| author_facet | Saik, Amy Yi Hsan Lim, Yau Yan Stanslas, Johnson Choo, Wee Sim |
| author_sort | Saik, Amy Yi Hsan |
| collection | UPM |
| description | Acylation of quercetin with cinnamic acid catalyzed by Candida antarctica lipase B (CAL-B) or Pseudomonas cepacia lipase C (PCL-C) was investigated. Specifically, the effects of reaction duration, incubation temperature, and molar ratio of substrates on bioconversion yield, initial rate of reaction, and regioselectivity were investigated. Three new acylated quercetin analogues were produced: quercetin 4′-cinnamate (C24H16O8), quercetin 3′,4′-dicinnamate (C33H22O9), and quercetin 7,3′,4′-tricinnamate (C42H28O10). The effects of the lipase-catalyzed acylation conditions on the bioconversion yields varied across the conditions. The initial rate of reaction of acylation of quercetin with cinnamic acid catalyzed by CAL-B and PCL-C was similar. In the presence of CAL-B, acylation mainly took place at the C-4′-OH, generating mostly quercetin 4′-cinnamate; whereas with PCL-C, acylation mainly took place at both the 4′- and 3′-hydroxyls, generating quercetin 3′,4′-dicinnamate. Thin-layer-chromatography analysis showed that the three acylated quercetin analogues had higher lipophilicity when compared with quercetin. In silico investigation revealed that quercetin 4’-cinnamate and quercetin 3′,4′-dicinnamate are likely to be orally active pharmacological drugs. |
| first_indexed | 2024-03-06T09:21:24Z |
| format | Article |
| id | upm.eprints-54718 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T09:21:24Z |
| publishDate | 2016 |
| publisher | Taylor & Francis |
| record_format | dspace |
| spelling | upm.eprints-547182018-04-19T07:59:57Z http://psasir.upm.edu.my/id/eprint/54718/ Lipase-catalyzed acylation of quercetin with cinnamic acid Saik, Amy Yi Hsan Lim, Yau Yan Stanslas, Johnson Choo, Wee Sim Acylation of quercetin with cinnamic acid catalyzed by Candida antarctica lipase B (CAL-B) or Pseudomonas cepacia lipase C (PCL-C) was investigated. Specifically, the effects of reaction duration, incubation temperature, and molar ratio of substrates on bioconversion yield, initial rate of reaction, and regioselectivity were investigated. Three new acylated quercetin analogues were produced: quercetin 4′-cinnamate (C24H16O8), quercetin 3′,4′-dicinnamate (C33H22O9), and quercetin 7,3′,4′-tricinnamate (C42H28O10). The effects of the lipase-catalyzed acylation conditions on the bioconversion yields varied across the conditions. The initial rate of reaction of acylation of quercetin with cinnamic acid catalyzed by CAL-B and PCL-C was similar. In the presence of CAL-B, acylation mainly took place at the C-4′-OH, generating mostly quercetin 4′-cinnamate; whereas with PCL-C, acylation mainly took place at both the 4′- and 3′-hydroxyls, generating quercetin 3′,4′-dicinnamate. Thin-layer-chromatography analysis showed that the three acylated quercetin analogues had higher lipophilicity when compared with quercetin. In silico investigation revealed that quercetin 4’-cinnamate and quercetin 3′,4′-dicinnamate are likely to be orally active pharmacological drugs. Taylor & Francis 2016 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/54718/1/Lipase-catalyzed%20acylation%20of%20quercetin%20with%20cinnamic%20acid.pdf Saik, Amy Yi Hsan and Lim, Yau Yan and Stanslas, Johnson and Choo, Wee Sim (2016) Lipase-catalyzed acylation of quercetin with cinnamic acid. Biocatalysis and Biotransformation, 34 (1). pp. 33-43. ISSN 1024-2422; ESSN: 1029-2446 https://www.tandfonline.com/doi/abs/10.1080/10242422.2016.1212844?journalCode=ibab20 10.1080/10242422.2016.1212844 |
| spellingShingle | Saik, Amy Yi Hsan Lim, Yau Yan Stanslas, Johnson Choo, Wee Sim Lipase-catalyzed acylation of quercetin with cinnamic acid |
| title | Lipase-catalyzed acylation of quercetin with cinnamic acid |
| title_full | Lipase-catalyzed acylation of quercetin with cinnamic acid |
| title_fullStr | Lipase-catalyzed acylation of quercetin with cinnamic acid |
| title_full_unstemmed | Lipase-catalyzed acylation of quercetin with cinnamic acid |
| title_short | Lipase-catalyzed acylation of quercetin with cinnamic acid |
| title_sort | lipase catalyzed acylation of quercetin with cinnamic acid |
| url | http://psasir.upm.edu.my/id/eprint/54718/1/Lipase-catalyzed%20acylation%20of%20quercetin%20with%20cinnamic%20acid.pdf |
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