新型油酸水合酶的生物催化研究

Q2 Chemical Engineering
Jens Schmid , Lisa Steiner , Silvia Fademrecht, Jürgen Pleiss, Konrad B. Otte, Bernhard Hauer
{"title":"新型油酸水合酶的生物催化研究","authors":"Jens Schmid ,&nbsp;Lisa Steiner ,&nbsp;Silvia Fademrecht,&nbsp;Jürgen Pleiss,&nbsp;Konrad B. Otte,&nbsp;Bernhard Hauer","doi":"10.1016/j.molcatb.2017.01.010","DOIUrl":null,"url":null,"abstract":"<div><p>The direct hydration of C<img>C bonds to yield alcohols or the reverse dehydration is chemically challenging but highly sought after. Recently, oleate hydratases (OAHs) gained attention as biocatalytic alternatives capable of hydrating isolated, non-activated C<img>C bonds. Their natural reaction is the conversion of oleic acid to (<em>R</em>)-10-hydroxystearic acid.</p><p>In this work, we report the first comparative study of several OAHs. Therefore we established the <em>Hydratase Engineering Database</em> (HyED) comprising 2046 putative OAHs from eleven homologous families and selected nine homologs for cloning in <em>E. coli</em>. The heterologously expressed enzymes were evaluated concerning activity and substrate specificity. The enzymes have a broad substrate scope ranging from oleic acid (C18) to the novel synthetic substrate (<em>Z</em>)-undec-9-enoic acid (C11). The OAHs from <em>Elizabethkingia meningoseptica</em> and <em>Chryseobacterium gleum</em> showed the best expression, highest stability and broadest substrate scope, making them interesting candidates for directed evolution to engineer them for the application as general hydratase catalysts.</p></div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S243-S249"},"PeriodicalIF":0.0000,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2017.01.010","citationCount":"24","resultStr":"{\"title\":\"Biocatalytic study of novel oleate hydratases\",\"authors\":\"Jens Schmid ,&nbsp;Lisa Steiner ,&nbsp;Silvia Fademrecht,&nbsp;Jürgen Pleiss,&nbsp;Konrad B. Otte,&nbsp;Bernhard Hauer\",\"doi\":\"10.1016/j.molcatb.2017.01.010\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The direct hydration of C<img>C bonds to yield alcohols or the reverse dehydration is chemically challenging but highly sought after. Recently, oleate hydratases (OAHs) gained attention as biocatalytic alternatives capable of hydrating isolated, non-activated C<img>C bonds. Their natural reaction is the conversion of oleic acid to (<em>R</em>)-10-hydroxystearic acid.</p><p>In this work, we report the first comparative study of several OAHs. Therefore we established the <em>Hydratase Engineering Database</em> (HyED) comprising 2046 putative OAHs from eleven homologous families and selected nine homologs for cloning in <em>E. coli</em>. The heterologously expressed enzymes were evaluated concerning activity and substrate specificity. The enzymes have a broad substrate scope ranging from oleic acid (C18) to the novel synthetic substrate (<em>Z</em>)-undec-9-enoic acid (C11). The OAHs from <em>Elizabethkingia meningoseptica</em> and <em>Chryseobacterium gleum</em> showed the best expression, highest stability and broadest substrate scope, making them interesting candidates for directed evolution to engineer them for the application as general hydratase catalysts.</p></div>\",\"PeriodicalId\":16416,\"journal\":{\"name\":\"Journal of Molecular Catalysis B-enzymatic\",\"volume\":\"133 \",\"pages\":\"Pages S243-S249\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2016-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/j.molcatb.2017.01.010\",\"citationCount\":\"24\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Molecular Catalysis B-enzymatic\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1381117717300103\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"Chemical Engineering\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Catalysis B-enzymatic","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1381117717300103","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"Chemical Engineering","Score":null,"Total":0}
引用次数: 24

摘要

CC键直接水合生成醇或反脱水在化学上具有挑战性,但备受追捧。最近,油酸水合酶(OAHs)作为一种能够水合分离的、非活化的CC键的生物催化剂引起了人们的关注。它们的自然反应是油酸转化为(R)-10-羟基硬脂酸。在这项工作中,我们报告了几种OAHs的首次比较研究。为此,我们建立了水合酶工程数据库(HyED),包括来自11个同源家族的2046个推定的OAHs,并选择了9个同源物在大肠杆菌中进行克隆。对异种表达酶的活性和底物特异性进行了评价。该酶具有广泛的底物范围,从油酸(C18)到新型合成底物(Z)-十一-9-烯酸(C11)。来自elizabeth ethkingia meningoseptica和Chryseobacterium gleum的OAHs表现出最好的表达,最高的稳定性和最广泛的底物范围,使它们成为定向进化的有趣候选物,以设计它们作为一般水合酶催化剂的应用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Biocatalytic study of novel oleate hydratases

Biocatalytic study of novel oleate hydratases

The direct hydration of CC bonds to yield alcohols or the reverse dehydration is chemically challenging but highly sought after. Recently, oleate hydratases (OAHs) gained attention as biocatalytic alternatives capable of hydrating isolated, non-activated CC bonds. Their natural reaction is the conversion of oleic acid to (R)-10-hydroxystearic acid.

In this work, we report the first comparative study of several OAHs. Therefore we established the Hydratase Engineering Database (HyED) comprising 2046 putative OAHs from eleven homologous families and selected nine homologs for cloning in E. coli. The heterologously expressed enzymes were evaluated concerning activity and substrate specificity. The enzymes have a broad substrate scope ranging from oleic acid (C18) to the novel synthetic substrate (Z)-undec-9-enoic acid (C11). The OAHs from Elizabethkingia meningoseptica and Chryseobacterium gleum showed the best expression, highest stability and broadest substrate scope, making them interesting candidates for directed evolution to engineer them for the application as general hydratase catalysts.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Journal of Molecular Catalysis B-enzymatic
Journal of Molecular Catalysis B-enzymatic 生物-生化与分子生物学
CiteScore
2.58
自引率
0.00%
发文量
0
审稿时长
3.4 months
期刊介绍: Journal of Molecular Catalysis B: Enzymatic is an international forum for researchers and product developers in the applications of whole-cell and cell-free enzymes as catalysts in organic synthesis. Emphasis is on mechanistic and synthetic aspects of the biocatalytic transformation. Papers should report novel and significant advances in one or more of the following topics; Applied and fundamental studies of enzymes used for biocatalysis; Industrial applications of enzymatic processes, e.g. in fine chemical synthesis; Chemo-, regio- and enantioselective transformations; Screening for biocatalysts; Integration of biocatalytic and chemical steps in organic syntheses; Novel biocatalysts, e.g. enzymes from extremophiles and catalytic antibodies; Enzyme immobilization and stabilization, particularly in non-conventional media; Bioprocess engineering aspects, e.g. membrane bioreactors; Improvement of catalytic performance of enzymes, e.g. by protein engineering or chemical modification; Structural studies, including computer simulation, relating to substrate specificity and reaction selectivity; Biomimetic studies related to enzymatic transformations.
×
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