Immobilized Fe3O4-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 Fe3O4 nanoparticles (Fe3O4-PDA-TLL). The behavior investigation revealed tha...

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Autores principales:	Zhaoyu Wang, Yang Li, Mingyi Li, Xiaohui Zhang, Qingxia Ji, Xiaojuan Zhao, Yanhong Bi, Si Luo
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	flavonoid glycosides immobilized enzyme magnetic nanoparticle Thermomyces lanuginosus lipase substrate recognition Biotechnology TP248.13-248.65
Acceso en línea:	https://doaj.org/article/38d63febad22490882336306845c8e02
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spelling	oai:doaj.org-article:38d63febad22490882336306845c8e022021-11-16T07:36:42ZImmobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition2296-418510.3389/fbioe.2021.798594https://doaj.org/article/38d63febad22490882336306845c8e022021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fbioe.2021.798594/fullhttps://doaj.org/toc/2296-4185The 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 Fe3O4 nanoparticles (Fe3O4-PDA-TLL). The behavior investigation revealed that Fe3O4-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, Fe3O4-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.Zhaoyu WangYang LiMingyi LiXiaohui ZhangQingxia JiXiaojuan ZhaoYanhong BiSi LuoFrontiers Media S.A.articleflavonoid glycosidesimmobilized enzymemagnetic nanoparticleThermomyces lanuginosus lipasesubstrate recognitionBiotechnologyTP248.13-248.65ENFrontiers in Bioengineering and Biotechnology, Vol 9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	flavonoid glycosides immobilized enzyme magnetic nanoparticle Thermomyces lanuginosus lipase substrate recognition Biotechnology TP248.13-248.65
spellingShingle	flavonoid glycosides immobilized enzyme magnetic nanoparticle Thermomyces lanuginosus lipase substrate recognition Biotechnology TP248.13-248.65 Zhaoyu Wang Yang Li Mingyi Li Xiaohui Zhang Qingxia Ji Xiaojuan Zhao Yanhong Bi Si Luo Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
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 Fe3O4 nanoparticles (Fe3O4-PDA-TLL). The behavior investigation revealed that Fe3O4-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, Fe3O4-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.
format	article
author	Zhaoyu Wang Yang Li Mingyi Li Xiaohui Zhang Qingxia Ji Xiaojuan Zhao Yanhong Bi Si Luo
author_facet	Zhaoyu Wang Yang Li Mingyi Li Xiaohui Zhang Qingxia Ji Xiaojuan Zhao Yanhong Bi Si Luo
author_sort	Zhaoyu Wang
title	Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_short	Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_full	Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_fullStr	Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_full_unstemmed	Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition
title_sort	immobilized fe3o4-polydopamine-thermomyces lanuginosus lipase-catalyzed acylation of flavonoid glycosides and their analogs: an improved insight into enzymic substrate recognition
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/38d63febad22490882336306845c8e02
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Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition

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