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固定化氧化亚铁-聚多巴胺-脂肪酶催化类黄酮糖苷及其类似物的酰化反应:对酶促底物识别的深入洞察。

Immobilized FeO-Polydopamine- Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition.

作者信息

Wang Zhaoyu, Li Yang, Li Mingyi, Zhang Xiaohui, Ji Qingxia, Zhao Xiaojuan, Bi Yanhong, Luo Si

机构信息

School of Life Science and Food Engineering, Huaiyin Institute of Technology, Huai'an, China.

出版信息

Front Bioeng Biotechnol. 2021 Nov 16;9:798594. doi: 10.3389/fbioe.2021.798594. eCollection 2021.

Abstract

The conversion of flavonoid glycosides and their analogs to their lipophilic ester derivatives was developed by nanobiocatalysts from immobilizing lipase (TLL) on polydopamine-functionalized magnetic FeO nanoparticles (FeO-PDA-TLL). The behavior investigation revealed that FeO-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, FeO-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.

摘要

通过将脂肪酶(TLL)固定在聚多巴胺功能化磁性FeO纳米颗粒(FeO-PDA-TLL)上制备的纳米生物催化剂,实现了类黄酮糖苷及其类似物向其亲脂性酯衍生物的转化。行为研究表明,FeO-PDA-TLL对长链脂肪酸(即C10至C14)表现出偏好,反应速率较高,为12.6 - 13.9 mM/h。关于底物特异性,FeO-PDA-TLL显示出良好的底物谱,并对伯羟基进行了有利的功能化,这表明空间位阻阻碍了底物的仲羟基或酚羟基进入TLL活性区域的结合位点以生成产物。

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