Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner
文献类型：期刊论文
| 作者 | Chen, Huayou1,2; Chen, Zhi1; Ni, Zhong1; Tian, Rui1; Zhang, Tianxi1; Jia, Jinru1; Chen, Keping1; Yang, Shengli1 |
| 刊名 | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
 |
| 出版日期 | 2016 |
| 卷号 | 123期号:JAN页码:73-80 |
| 关键词 | Nitrilase B. subtilis Spore surface display Enzyme immobilization |
| ISSN号 | 1381-1177 |
| 通讯作者 | Chen, HY (reprint author), Jiangsu Univ, Inst Life Sci, Xuefu Rd 301, Zhenjiang 212000, Peoples R China. |
| 英文摘要 | In the present study, probiotic Bacillus spores were used as a matrix for enzyme immobilization, because of their inherent resistance to extreme temperatures, UV irradiation, solvents and drying. An Escherichia coli- Bacillus subtilis shuttle vector (pHS-CotG-nit) was constructed for the spore surface display of the nitrilase from hyperthermophilic bacterium Thermotoga maritima MSB8. The successful display of CotG-nit fusion protein on the spore surface of B. subtilis was verified by western blot analysis and activity measurement. The optimal temperature and pH of the spore surface-dispalyed nitrilase were observed to be 50 degrees C and pH 8.0, respectively, which were higher than the free nitrilase (45 degrees C and pH 7.5). The analysis of thermal and pH stability indicated that the spore surface-displayed nitrilase retained 79% and 97% at 75 degrees C and pH 8.0 after 1 h of incubation, whereas it were 32% and 52%, respectively, for free nitrilase. Furthermore, the reusability experiments indicated that the activity of the spore surface displayed nitrilase was not significantly decreased throughout the reusability process, which still retained 83% of the initial activity at the fifth cycle. Above all, these results suggested that surface display of enzymes on the spore of B. subtilis might be an effective method for enzyme immobilization and help to meet the ever-increasing industrial demand for preparation and stabilization of biocatalysts. (C) 2015 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] | BIOCHEMICAL-CHARACTERIZATION ; EFFICIENT PRODUCTION ; BIOCATALYSIS ; IMMOBILIZATION ; SYSTEM ; HYDROLYSIS ; RESISTANCE ; LACCASE ; ENZYME ; CELLS |
| 收录类别 | SCI |
| 原文出处 | ELSEVIER SCIENCE BV |
| 语种 | 英语 |
| WOS记录号 | WOS:000369681800012 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/20655]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.Jiangsu Univ, Inst Life Sci, Xuefu Rd 301, Zhenjiang 212000, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing, Peoples R China |
| 推荐引用方式 GB/T 7714 | Chen, Huayou,Chen, Zhi,Ni, Zhong,et al. Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2016,123(JAN):73-80. |
| APA | Chen, Huayou.,Chen, Zhi.,Ni, Zhong.,Tian, Rui.,Zhang, Tianxi.,...&Yang, Shengli.(2016).Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,123(JAN),73-80. |
| MLA | Chen, Huayou,et al."Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 123.JAN(2016):73-80. |
入库方式： OAI收割
来源：过程工程研究所
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