Immobilization and interfacial activation of lipase at liquid and solid interfaces.

IF 2.9 3区 化学 Q3 CHEMISTRY, PHYSICAL
Soft Matter Pub Date : 2025-03-10 DOI:10.1039/d4sm01218f
P Giefer, U Fritsching, L Colombi Ciacchi, S Köppen-Hannemann
{"title":"Immobilization and interfacial activation of lipase at liquid and solid interfaces.","authors":"P Giefer, U Fritsching, L Colombi Ciacchi, S Köppen-Hannemann","doi":"10.1039/d4sm01218f","DOIUrl":null,"url":null,"abstract":"<p><p>This study investigates the adsorption behaviour of <i>Candida rugosa</i> lipase at silica/water and oil/water interfaces by means of molecular dynamics simulations. The findings reveal distinct adsorption orientations and structural differences that can be related to different enzymatic activities and selectivities. At the silica/water interface, lipase adsorbs with the LID region facing the solvent, in a configuration that is not fully open, but still grants access to its catalytic triad, as shown by tunnel calculations. These also reveal the presence of two ester-exit tunnels, suggesting a high catalytic turnover capability of the adsorbed enzyme. Docking simulations predict binding of triacylglyceride substrates with marked selectivity regarding the length of the hydrophobic chains and the substrate chirality. At the oil/water interface, lipase adsorbs <i>via</i> the LID region with widely open ingress tunnels, facilitating direct substrate extraction from the interface. The two opposite adsorption orientations allow favorable interactions of silica-immobilized lipase with oil droplets that cause no appreciable change in the conformation, activity, or selectivity. These results provide a molecular-scale rationalization of the lipid hydrolysis mechanisms that support the deployment of lipase immobilized in ceramic membranes for lipolytic applications.</p>","PeriodicalId":103,"journal":{"name":"Soft Matter","volume":" ","pages":""},"PeriodicalIF":2.9000,"publicationDate":"2025-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Soft Matter","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1039/d4sm01218f","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 0

Abstract

This study investigates the adsorption behaviour of Candida rugosa lipase at silica/water and oil/water interfaces by means of molecular dynamics simulations. The findings reveal distinct adsorption orientations and structural differences that can be related to different enzymatic activities and selectivities. At the silica/water interface, lipase adsorbs with the LID region facing the solvent, in a configuration that is not fully open, but still grants access to its catalytic triad, as shown by tunnel calculations. These also reveal the presence of two ester-exit tunnels, suggesting a high catalytic turnover capability of the adsorbed enzyme. Docking simulations predict binding of triacylglyceride substrates with marked selectivity regarding the length of the hydrophobic chains and the substrate chirality. At the oil/water interface, lipase adsorbs via the LID region with widely open ingress tunnels, facilitating direct substrate extraction from the interface. The two opposite adsorption orientations allow favorable interactions of silica-immobilized lipase with oil droplets that cause no appreciable change in the conformation, activity, or selectivity. These results provide a molecular-scale rationalization of the lipid hydrolysis mechanisms that support the deployment of lipase immobilized in ceramic membranes for lipolytic applications.

脂肪酶在液体和固体界面的固定化和界面活化。
采用分子动力学模拟的方法研究了念珠菌脂肪酶在二氧化硅/水界面和油水界面的吸附行为。研究结果表明,不同的吸附取向和结构差异可能与不同的酶活性和选择性有关。在二氧化硅/水界面上,脂肪酶与面向溶剂的LID区域吸附,其结构不是完全开放的,但仍然允许进入其催化三元组,如隧道计算所示。这些还揭示了两个酯出口通道的存在,表明吸附酶具有高的催化周转能力。对接模拟预测三酰甘油底物的结合对疏水链的长度和底物的手性具有显著的选择性。在油水界面处,脂肪酶通过具有广泛开放入口通道的LID区域吸附,便于从界面直接提取底物。两种相反的吸附方向允许硅固定化脂肪酶与油滴良好的相互作用,而不会引起构象、活性或选择性的明显变化。这些结果为脂质水解机制提供了分子尺度上的合理化,支持了固定化脂肪酶在陶瓷膜上的应用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Soft Matter
Soft Matter 工程技术-材料科学:综合
CiteScore
6.00
自引率
5.90%
发文量
891
审稿时长
1.9 months
期刊介绍: Soft Matter is an international journal published by the Royal Society of Chemistry using Engineering-Materials Science: A Synthesis as its research focus. It publishes original research articles, review articles, and synthesis articles related to this field, reporting the latest discoveries in the relevant theoretical, practical, and applied disciplines in a timely manner, and aims to promote the rapid exchange of scientific information in this subject area. The journal is an open access journal. The journal is an open access journal and has not been placed on the alert list in the last three years.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信