Immobilized Fe(3)O(4)-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition

The conversion of flavonoid glycosides and their analogs to their lipophilic ester derivatives was developed by nanobiocatalysts from immobilizing Thermomyces lanuginosus lipase (TLL) on polydopamine-functionalized magnetic Fe(3)O(4) nanoparticles (Fe(3)O(4)-PDA-TLL). The behavior investigation reve...

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Detalles Bibliográficos
Autores principales: Wang, Zhaoyu, Li, Yang, Li, Mingyi, Zhang, Xiaohui, Ji, Qingxia, Zhao, Xiaojuan, Bi, Yanhong, Luo, Si
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Bioengineering and Biotechnology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8636704/
https://www.ncbi.nlm.nih.gov/pubmed/34869302
http://dx.doi.org/10.3389/fbioe.2021.798594
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author Wang, Zhaoyu
Li, Yang
Li, Mingyi
Zhang, Xiaohui
Ji, Qingxia
Zhao, Xiaojuan
Bi, Yanhong
Luo, Si
author_facet Wang, Zhaoyu
Li, Yang
Li, Mingyi
Zhang, Xiaohui
Ji, Qingxia
Zhao, Xiaojuan
Bi, Yanhong
Luo, Si
author_sort Wang, Zhaoyu
collection PubMed
description The conversion of flavonoid glycosides and their analogs to their lipophilic ester derivatives was developed by nanobiocatalysts from immobilizing Thermomyces lanuginosus lipase (TLL) on polydopamine-functionalized magnetic Fe(3)O(4) nanoparticles (Fe(3)O(4)-PDA-TLL). The behavior investigation revealed that Fe(3)O(4)-PDA-TLL exhibits a preference for long chain length fatty acids (i.e., C10 to C14) with higher reaction rates of 12.6–13.9 mM/h. Regarding the substrate specificity, Fe(3)O(4)-PDA-TLL showed good substrate spectrum and favorably functionalized the primary OH groups, suggesting that the steric hindrances impeded the secondary or phenolic hydroxyl groups of substrates into the bonding site of the active region of TLL to afford the product.
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spelling pubmed-86367042021-12-03 Immobilized Fe(3)O(4)-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition Wang, Zhaoyu Li, Yang Li, Mingyi Zhang, Xiaohui Ji, Qingxia Zhao, Xiaojuan Bi, Yanhong Luo, Si Front Bioeng Biotechnol Bioengineering and Biotechnology The conversion of flavonoid glycosides and their analogs to their lipophilic ester derivatives was developed by nanobiocatalysts from immobilizing Thermomyces lanuginosus lipase (TLL) on polydopamine-functionalized magnetic Fe(3)O(4) nanoparticles (Fe(3)O(4)-PDA-TLL). The behavior investigation revealed that Fe(3)O(4)-PDA-TLL exhibits a preference for long chain length fatty acids (i.e., C10 to C14) with higher reaction rates of 12.6–13.9 mM/h. Regarding the substrate specificity, Fe(3)O(4)-PDA-TLL showed good substrate spectrum and favorably functionalized the primary OH groups, suggesting that the steric hindrances impeded the secondary or phenolic hydroxyl groups of substrates into the bonding site of the active region of TLL to afford the product. Frontiers Media S.A. 2021-11-16 /pmc/articles/PMC8636704/ /pubmed/34869302 http://dx.doi.org/10.3389/fbioe.2021.798594 Text en Copyright © 2021 Wang, Li, Li, Zhang, Ji, Zhao, Bi and Luo. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Bioengineering and Biotechnology
Wang, Zhaoyu
Li, Yang
Li, Mingyi
Zhang, Xiaohui
Ji, Qingxia
Zhao, Xiaojuan
Bi, Yanhong
Luo, Si
Immobilized Fe(3)O(4)-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title Immobilized Fe(3)O(4)-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_full Immobilized Fe(3)O(4)-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_fullStr Immobilized Fe(3)O(4)-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_full_unstemmed Immobilized Fe(3)O(4)-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_short Immobilized Fe(3)O(4)-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_sort immobilized fe(3)o(4)-polydopamine-thermomyces lanuginosus lipase-catalyzed acylation of flavonoid glycosides and their analogs: an improved insight into enzymic substrate recognition
topic Bioengineering and Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8636704/
https://www.ncbi.nlm.nih.gov/pubmed/34869302
http://dx.doi.org/10.3389/fbioe.2021.798594
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