Enzymatic hydrogenation of diverse activated alkenes. Identification of two Bacillus old yellow enzymes with broad substrate profiles
文献类型：期刊论文
| 作者 | Zhang, Hailing1,2,3; Gao, Xiuzhen2,3; Ren, Jie2,3; Feng, Jinhui2,3; Zhang, Tongcun1; Wu, Qiaqing2,3; Zhu, Dunming2,3 |
| 刊名 | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
 |
| 出版日期 | 2014-07-01 |
| 卷号 | 105页码:118-125 |
| 关键词 | Ene-reductase Old yellow enzyme Reduction of alkenes Biocatalytic hydrogenation Substrate specificity |
| 英文摘要 | By whole cell transformation, 32 out of 71 strains showed OYEs activity toward maleimide in the first round screening. Among them, a Bacillus strain was identified to be active toward a selection of substrates with different electron-withdrawing groups. Two OYE homologous genes, bac-oye1 and bac-oye2 were cloned from this strain and overexpressed in Escherichia coli BL21(DE3). The recombinant enzyme Bac-OYE2 showed a broader pH range (6.0-10.5), while Bac-OYE1 was so sensitive to pH that it lost most of the enzyme activity below pH 6.0 or above pH 9.0. The reaction temperature exerted similar effects on the activities of both enzymes, but the stability of Bac-OYE2 was more sensitive to the temperature than Bac-OYE1. In addition to alpha,beta-unsaturated aldehydes, ketones, nitroalkenes, and the double activated carboxylic acids, esters, nitrites and cyclicimides, Bac-OYE1 and Bac-OYE2 also exhibited activities toward the "borderline" substrates such as unsaturated lactones, mono carboxylic esters, showing their broader substrate scopes. These enzymes also had excellent enantioselectivity as evidenced by the reductions of several alpha,beta-unsaturated cyclic ketones, a-substituted alpha,beta-unsaturated carboxylic esters and 2-methyl maleimide. For example, methyl 2-acetamidoacrylate was reduced by Bac-OYE1 with >99% conversion and >99% ee. (c) 2014 Elsevier B.V. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
| 类目[WOS] | Biochemistry & Molecular Biology ; Chemistry, Physical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
| 关键词[WOS] | ASYMMETRIC BIOREDUCTION ; C=C BONDS ; ENOATE REDUCTASES ; REDUCTION ; FAMILY ; PROTEIN ; TOMATO |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000337551900017 |
| 源URL | [http://124.16.173.210/handle/834782/1410]  |
| 专题 | 天津工业生物技术研究所_生物催化与绿色化工 朱敦明_期刊论文 |
| 作者单位 | 1.Tianjin Univ Sci & Technol, Coll Bioengn, Tianjin 300457, Peoples R China 2.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Lab Ind Enzymes, Tianjin 300308, Peoples R China 3.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin Engn Ctr Biocatalyt Technol, Tianjin 300308, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Hailing,Gao, Xiuzhen,Ren, Jie,et al. Enzymatic hydrogenation of diverse activated alkenes. Identification of two Bacillus old yellow enzymes with broad substrate profiles[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2014,105:118-125. |
| APA | Zhang, Hailing.,Gao, Xiuzhen.,Ren, Jie.,Feng, Jinhui.,Zhang, Tongcun.,...&Zhu, Dunming.(2014).Enzymatic hydrogenation of diverse activated alkenes. Identification of two Bacillus old yellow enzymes with broad substrate profiles.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,105,118-125. |
| MLA | Zhang, Hailing,et al."Enzymatic hydrogenation of diverse activated alkenes. Identification of two Bacillus old yellow enzymes with broad substrate profiles".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 105(2014):118-125. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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