Bioinspired Lipase Immobilized Membrane for Improving Hesperidin Lipophilization
Lipophilization is a promising way to improve the bioavailability of flavonoids. However, the traditional enzymatic esterification methods are time-consuming, and present low yields and purity. Herein, a novel membrane-based lipophilization technology—bioinspired lipase immobilized membranes (BLIMs)...
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ftdoajarticles:oai:doaj.org/article:1c9c4b0227984fc5a1cdfc891b23c6cc 2023-08-27T04:06:03+02:00 Bioinspired Lipase Immobilized Membrane for Improving Hesperidin Lipophilization Shanxiu Ming Shuyi Li Zhe Chen Xujun Chen Feifei Wang Shaonan Deng Krystian Marszałek Zhenzhou Zhu Wenxiang Zhang Francisco J. Barba 2022-09-01T00:00:00Z https://doi.org/10.3390/antiox11101906 https://doaj.org/article/1c9c4b0227984fc5a1cdfc891b23c6cc EN eng MDPI AG https://www.mdpi.com/2076-3921/11/10/1906 https://doaj.org/toc/2076-3921 doi:10.3390/antiox11101906 2076-3921 https://doaj.org/article/1c9c4b0227984fc5a1cdfc891b23c6cc Antioxidants, Vol 11, Iss 1906, p 1906 (2022) Candida antarctica lipase B enzymatic esterification membrane separation hesperidin lipophilization bioinspired lipase immobilized membrane Therapeutics. Pharmacology RM1-950 article 2022 ftdoajarticles https://doi.org/10.3390/antiox11101906 2023-08-06T00:42:23Z Lipophilization is a promising way to improve the bioavailability of flavonoids. However, the traditional enzymatic esterification methods are time-consuming, and present low yields and purity. Herein, a novel membrane-based lipophilization technology—bioinspired lipase immobilized membranes (BLIMs), including CAL-B@PES, CAL-B@PDA/PES and GA/CAL-B@PDA/PES— were fabricated to improve the antioxidant flavanone glycoside hesperidin lipophilization. Via reverse filtration, PDA coating and GA crosslinking, Candida antarctica lipase B (CAL-B) was stably immobilized on membrane to fabricate BLIMs. Among the three BLIMs, GA/CAL-B@PDA/PES had the greatest enzyme activity and enzyme loading, the strongest tolerance of changes in external environmental conditions (temperatures, pH, heating time, storage time and numbers of cycles) and the highest hesperidin esterification efficiency. Moreover, the optimal operating condition for GA/CAL-B@PDA/PES fabrication was the CAL-B concentration of 0.36 mg/mL, operation pressure of 2 bar, GA concentration of 5% and crosslinking time of 1 h. Afterwards, the hesperidin esterification process did not affect the micromorphology of BLIM, but clearly improved the BLIM permeability and esterified product efficiency. The present study reveals the fabrication mechanism of BLIMs and offers insights into the optimizing strategy that governs the membrane-based lipophilization technology process. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Antioxidants 11 10 1906 |
institution |
Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Candida antarctica lipase B enzymatic esterification membrane separation hesperidin lipophilization bioinspired lipase immobilized membrane Therapeutics. Pharmacology RM1-950 |
spellingShingle |
Candida antarctica lipase B enzymatic esterification membrane separation hesperidin lipophilization bioinspired lipase immobilized membrane Therapeutics. Pharmacology RM1-950 Shanxiu Ming Shuyi Li Zhe Chen Xujun Chen Feifei Wang Shaonan Deng Krystian Marszałek Zhenzhou Zhu Wenxiang Zhang Francisco J. Barba Bioinspired Lipase Immobilized Membrane for Improving Hesperidin Lipophilization |
topic_facet |
Candida antarctica lipase B enzymatic esterification membrane separation hesperidin lipophilization bioinspired lipase immobilized membrane Therapeutics. Pharmacology RM1-950 |
description |
Lipophilization is a promising way to improve the bioavailability of flavonoids. However, the traditional enzymatic esterification methods are time-consuming, and present low yields and purity. Herein, a novel membrane-based lipophilization technology—bioinspired lipase immobilized membranes (BLIMs), including CAL-B@PES, CAL-B@PDA/PES and GA/CAL-B@PDA/PES— were fabricated to improve the antioxidant flavanone glycoside hesperidin lipophilization. Via reverse filtration, PDA coating and GA crosslinking, Candida antarctica lipase B (CAL-B) was stably immobilized on membrane to fabricate BLIMs. Among the three BLIMs, GA/CAL-B@PDA/PES had the greatest enzyme activity and enzyme loading, the strongest tolerance of changes in external environmental conditions (temperatures, pH, heating time, storage time and numbers of cycles) and the highest hesperidin esterification efficiency. Moreover, the optimal operating condition for GA/CAL-B@PDA/PES fabrication was the CAL-B concentration of 0.36 mg/mL, operation pressure of 2 bar, GA concentration of 5% and crosslinking time of 1 h. Afterwards, the hesperidin esterification process did not affect the micromorphology of BLIM, but clearly improved the BLIM permeability and esterified product efficiency. The present study reveals the fabrication mechanism of BLIMs and offers insights into the optimizing strategy that governs the membrane-based lipophilization technology process. |
format |
Article in Journal/Newspaper |
author |
Shanxiu Ming Shuyi Li Zhe Chen Xujun Chen Feifei Wang Shaonan Deng Krystian Marszałek Zhenzhou Zhu Wenxiang Zhang Francisco J. Barba |
author_facet |
Shanxiu Ming Shuyi Li Zhe Chen Xujun Chen Feifei Wang Shaonan Deng Krystian Marszałek Zhenzhou Zhu Wenxiang Zhang Francisco J. Barba |
author_sort |
Shanxiu Ming |
title |
Bioinspired Lipase Immobilized Membrane for Improving Hesperidin Lipophilization |
title_short |
Bioinspired Lipase Immobilized Membrane for Improving Hesperidin Lipophilization |
title_full |
Bioinspired Lipase Immobilized Membrane for Improving Hesperidin Lipophilization |
title_fullStr |
Bioinspired Lipase Immobilized Membrane for Improving Hesperidin Lipophilization |
title_full_unstemmed |
Bioinspired Lipase Immobilized Membrane for Improving Hesperidin Lipophilization |
title_sort |
bioinspired lipase immobilized membrane for improving hesperidin lipophilization |
publisher |
MDPI AG |
publishDate |
2022 |
url |
https://doi.org/10.3390/antiox11101906 https://doaj.org/article/1c9c4b0227984fc5a1cdfc891b23c6cc |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Antioxidants, Vol 11, Iss 1906, p 1906 (2022) |
op_relation |
https://www.mdpi.com/2076-3921/11/10/1906 https://doaj.org/toc/2076-3921 doi:10.3390/antiox11101906 2076-3921 https://doaj.org/article/1c9c4b0227984fc5a1cdfc891b23c6cc |
op_doi |
https://doi.org/10.3390/antiox11101906 |
container_title |
Antioxidants |
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11 |
container_issue |
10 |
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1906 |
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