Enzymatic synthesis of 3-hydroxypropionic acid at high productivity by using free or immobilized cells of recombinant Escherichia coli
文献类型:期刊论文
作者 | Yu, Shanshan1,2,3; Yao, Peiyuan2,3; Li, Jianjiong2,3; Ren, Jie2,3; Yuan, Jing2,3; Feng, Jinhui2,3; Wang, Min1; Wu, Qiaqing2,3; Zhu, Dunming2,3 |
刊名 | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
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出版日期 | 2016-07-01 |
卷号 | 129页码:37-42 |
关键词 | Nitrilase Immobilization 3-Hydroxypropionic acid Hydrolysis Enzyme catalysis |
英文摘要 | 3-Hydroxypropionic acid (3-HP) is an important platform chemical for organic synthesis and high performance polymers. Despite a wealth of reports related to 3-HP biosynthesis in microorganisms, its industrial application still requires further research because of low titer and productivity. Herein an effective enzymatic method for the synthesis of 3-HP was achieved by using free or immobilized recombinant Escherichia coli BL21(DE3) cells harboring a nitrilase gene from environmental sample (NIT190). Under the optimal conditions (100 mmol/LTris-HCl buffer, pH 8.0, 30 degrees C), the maximum substrate concentration which could be completely hydrolyzed by using free cells within 24h was 4.5 mol/L (319.5 g/L). Furthermore, immobilization of the whole cells enhanced their substrate tolerance (up to 7.0 mol/L), stability, and reusability. The immobilized cells could be reused for up to 30 batches, and 70% of enzyme activity was retained after 74 batches in distilled water. The titer (184.7 g/L) and productivity (36.9 g/(Lh)) were obtained by isolation and purification of 3-HP from the first 30 batches. These results demonstrate that the immobilized cells have potential industrial application for the synthesis of 3-HP. (C) 2016 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] | GLYCEROL METABOLISM ; SACCHAROMYCES-CEREVISIAE ; LACTOBACILLUS-REUTERI ; NITRILASE ; TRANSFORMATION ; HYDROLYSIS ; PATHWAY ; INTERMEDIATE ; EFFICIENT |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000377729700006 |
源URL | [http://124.16.173.210/handle/834782/2905] ![]() |
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 Biotechnol, Minist Educ, Key Lab Ind Fermentat Microbiol, Tianjin 300457, Peoples R China 2.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Lab Ind Enzymes, Tianjin Airport Econ Area, 32 Xi Qi Dao, Tianjin 300308, Peoples R China 3.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin Engn Ctr Biocatalyt Technol, Tianjin Airport Econ Area, 32 Xi Qi Dao, Tianjin 300308, Peoples R China |
推荐引用方式 GB/T 7714 | Yu, Shanshan,Yao, Peiyuan,Li, Jianjiong,et al. Enzymatic synthesis of 3-hydroxypropionic acid at high productivity by using free or immobilized cells of recombinant Escherichia coli[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2016,129:37-42. |
APA | Yu, Shanshan.,Yao, Peiyuan.,Li, Jianjiong.,Ren, Jie.,Yuan, Jing.,...&Zhu, Dunming.(2016).Enzymatic synthesis of 3-hydroxypropionic acid at high productivity by using free or immobilized cells of recombinant Escherichia coli.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,129,37-42. |
MLA | Yu, Shanshan,et al."Enzymatic synthesis of 3-hydroxypropionic acid at high productivity by using free or immobilized cells of recombinant Escherichia coli".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 129(2016):37-42. |
入库方式: OAI收割
来源:天津工业生物技术研究所
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