A Chimeric Styrene Monooxygenase with Increased Efficiency in Asymmetric Biocatalytic Epoxidation

Corrado Maria L.; Knaus Tanja; Mutti Francesco G.

摘要

Abstract > The styrene monooxygenase (SMO) system from Pseudomonas sp. consists of two enzymes (StyA and StyB). StyB catalyses the reduction of FAD at the expense of NADH. After the transfer of FADH <sub>2</sub> from StyB to StyA, reaction with O <sub>2</sub> generates FAD‐OOH, which is the epoxidising agent. The wastage of redox equivalents due to partial diffusive transfer of FADH <sub>2</sub> , the insolubility of recombinant StyB and the impossibility of expressing StyA and StyB in a 1:1 molar ratio reduce the catalytic efficiency of the natural system. Herein we present a chimeric SMO (Fus‐SMO) that was obtained by genetic fusion of StyA and StyB through a flexible linker. Thanks to a combination of: 1)?balanced and improved expression levels of reductase and epoxidase units, and 2)?intrinsically higher specific epoxidation activity of Fus‐SMO in some cases, Escherichia coli cells expressing Fus‐SMO possess about 50?% higher activity for the epoxidation of styrene derivatives than E.?coli cells coexpressing StyA and StyB as discrete enzymes. The epoxidation activity of purified Fus‐SMO was up to three times higher than that of the two‐component StyA/StyB (1:1, molar ratio) system and up to 110 times higher than that of the natural fused SMO. Determination of coupling efficiency and study of the influence of O <sub>2</sub> pressure were also performed. Finally, Fus‐SMO and formate dehydrogenase were coexpressed in E.?coli and applied as a self‐sufficient biocatalytic system for epoxidation on greater than 500?mg scale. </abstract> </span> <span class="z_kbtn z_kbtnclass hoverxs" style="display: none;">展开▼</span> </div> <div class="translation abstracttxt"> <span class="zhankaihshouqi fivelineshidden" id="abstract"> <span>机译：</span><Abstract Type =“main”XML：Lang =“en”> <标题类型=“main”>摘录</标题> >来自假单胞菌的苯乙烯单氧基酶（Smo）系统</ i> sp。由两种酶（Stya和Styb）组成。 Styb催化了以牺牲NADH为代价的减少。从STYB转移FADH <sub> 2 </ sub>后，与O <sub> 2 </ sub>的反应产生FAD-OOH，即环氧化剂。氧化还原等同物的损害由于FADH <sub> 2 </ sub>，重组STY的不溶性和在1：1摩尔比中表达STYA和STYB的不可能性降低了天然系统的催化效率。在本文中，我们呈现了通过柔性接头通过STYA和STYB的遗传融合而获得的嵌合体液（FUS-SMO）。由于结合：1）？还原酶和环氧酶单位的平衡和改善的表达水平，2）？在某些情况下，FUS-Smo的本质上更高的特异性环氧化活性，大肠杆菌Coli </ i>表达Fus的细胞Smo对苯乙烯衍生物的环氧化的活性大约50？％，而不是<i.的E.?coli </ i>作为离散酶的细胞共存。纯化的FUS-Smo的环氧化活性高达3倍，高于双组分STYA / Styb（1：1，摩尔比）系统，高于天然融合液相色谱的110倍。还进行了偶联效率的测定以及O <SUB> 2 </ sub>压力的影响。最后，在 E.?CLI中共同施加Fus-Smo和甲酸脱氢酶，并施加作为自充足生物催化系统的用于环氧化，在大于500Ω·mg级。 </ p> </ abstract> </span> <span class="z_kbtn z_kbtnclass hoverxs" style="display: none;">展开▼</span> </div> </div> <div class="record"> <h2 class="all_title" id="enpatent33" >著录项</h2> <ul> <li> <span class="lefttit">来源</span> <div style="width: 86%;vertical-align: text-top;display: inline-block;"> <a href='/journal-foreign-16039/'>《Chembiochem: A European journal of chemical biology》</a> <b style="margin: 0 2px;">|</b><span>2018年第7期</span><b style="margin: 0 2px;">|</b><span>共8页</span> </div> </li> <li> <div class="author"> <span class="lefttit">作者</span> <p id="fAuthorthree" class="threelineshidden zhankaihshouqi"> <a href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=Corrado Maria L.&option=202" target="_blank" rel="nofollow">Corrado Maria L.;</a> <a href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=Knaus Tanja&option=202" target="_blank" rel="nofollow">Knaus Tanja;</a> <a href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=Mutti Francesco G.&option=202" target="_blank" rel="nofollow">Mutti Francesco G.;</a> </p> <span class="z_kbtnclass z_kbtnclassall hoverxs" id="zkzz" style="display: none;">展开▼</span> </div> </li> <li> <div style="display: flex;"> <span class="lefttit">作者单位</span> <div style="position: relative;margin-left: 3px;max-width: 639px;"> <div class="threelineshidden zhankaihshouqi" id="fOrgthree"> <p>Van't Hoff Institute for Molecular SciencesUniversity of AmsterdamScience Park 904 1098 XH Amsterdam The Netherlands;</p> <p>Van't Hoff Institute for Molecular SciencesUniversity of AmsterdamScience Park 904 1098 XH Amsterdam The Netherlands;</p> <p>Van't Hoff Institute for Molecular SciencesUniversity of AmsterdamScience Park 904 1098 XH Amsterdam The Netherlands;</p> </div> <span class="z_kbtnclass z_kbtnclassall hoverxs" id="zhdw" style="display: none;">展开▼</span> </div> </div> </li> <li > <span class="lefttit">收录信息</span> <span style="width: 86%;vertical-align: text-top;display: inline-block;"></span> </li> <li> <span class="lefttit">原文格式</span> <span>PDF</span> </li> <li> <span class="lefttit">正文语种</span> <span>eng</span> </li> <li> <span class="lefttit">中图分类</span> <span><a href="https://www.zhangqiaokeyan.com/clc/179.html" title="分子生物学">分子生物学;</a></span> </li> <li class="antistop"> <span class="lefttit">关键词</span> <p style="width: 86%;vertical-align: text-top;"> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=asymmetric synthesis&option=203" rel="nofollow">asymmetric synthesis;</a> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=biocatalysis&option=203" rel="nofollow">biocatalysis;</a> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=enzymatic fusion&option=203" rel="nofollow">enzymatic fusion;</a> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=epoxidation&option=203" rel="nofollow">epoxidation;</a> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=styrene monooxygenases&option=203" rel="nofollow">styrene monooxygenases;</a> </p> <div class="translation"> 机译：不对称合成;生物催化;酶融合;环氧化;苯乙烯单氧基酶; 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