@Robust enhancing stability and fructose tolerance of sucrose phosphorylase by immobilization on Ni-NTA functionalized agarose microspheres for the biosynthesis of 2-alpha-glucosylglycerol
文献类型：期刊论文
| 作者 | Xu, Haichang1,2; Wei, Bin1,2; Liu, Xiaojie1,2; Huang, Yongdong3; Zhou, Weiqing3,4; Liang, Hao1,2 |
| 刊名 | BIOCHEMICAL ENGINEERING JOURNAL
 |
| 出版日期 | 2022-03-01 |
| 卷号 | 180页码:9 |
| 关键词 | Sucrose phosphorylase Immobilization Agarose Stability Fructose tolerance |
| ISSN号 | 1369-703X |
| DOI | 10.1016/j.bej.2022.108362 |
| 英文摘要 | Sucrose phosphorylase (SPase) is a carbohydrate-active enzyme with outstanding potential for the biocatalytic conversion of sucrose and glycerol into 2-alpha-glucosylglycerol (2-alpha-GG) with attractive properties. However, poor stability, lack of appropriate immobilization strategy and serious inhibition of fructose by-products significantly restrict the industrial application of SPase. In this study, a new recombinant SPase from the Bifidobacterium Magian was specifically immobilized by agarose microspheres with Ni2+-nitrotriacetic acid for significantly enhancing its stability and fructose tolerance. Agarose immobilization greatly improved the stability of SPase. At 50 degrees C, the relative activity of the immobilized SPase (95%) was obviously greater than that of the free SPase (55%). Moreover, immobilized SPase exhibited excellent reusability and storage stability, retaining over 60% of its initial activity after 15 cycles, maintaining 70% relative activity after 15 days. It was first found that SPase immobilized by agamse still hold 98% activity even under 0.6 M fructose. Based on Raman spectrum analysis, agarose immobilization significantly enhanced the beta-sheet structures of SPase, which helped to maintain its efficient catalytic performance under extreme environment and high inhibitor concentration. Immobilized SPase based on agamse would have a brilliant future in the production of 2-alpha-GG. |
| WOS关键词 | SECONDARY STRUCTURE ; ENZYME ; GLUCOSYLGLYCEROL ; NANOPARTICLES ; RAMAN |
| 资助项目 | National Key Research and Development Program of China[2021YFC2102800] ; National Natural Science Foundation of China[21878014] ; National Natural Science Foundation of China[22078014] ; Hebei Key Research and Development Project[20372508D] |
| WOS研究方向 | Biotechnology & Applied Microbiology ; Engineering |
| 语种 | 英语 |
| WOS记录号 | WOS:000760987100001 |
| 出版者 | ELSEVIER |
| 资助机构 | National Key Research and Development Program of China ; National Natural Science Foundation of China ; Hebei Key Research and Development Project |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/52170]  |
| 专题 | 中国科学院过程工程研究所 |
| 通讯作者 | Zhou, Weiqing; Liang, Hao |
| 作者单位 | 1.Beijing Univ Chem Technol, State Key Lab Chem Resource Engn, Beijing 100029, Peoples R China 2.Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing 100029, Peoples R China 3.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China 4.Univ Chinese Acad Sci, Sch Chem Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Xu, Haichang,Wei, Bin,Liu, Xiaojie,et al. @Robust enhancing stability and fructose tolerance of sucrose phosphorylase by immobilization on Ni-NTA functionalized agarose microspheres for the biosynthesis of 2-alpha-glucosylglycerol[J]. BIOCHEMICAL ENGINEERING JOURNAL,2022,180:9. |
| APA | Xu, Haichang,Wei, Bin,Liu, Xiaojie,Huang, Yongdong,Zhou, Weiqing,&Liang, Hao.(2022).@Robust enhancing stability and fructose tolerance of sucrose phosphorylase by immobilization on Ni-NTA functionalized agarose microspheres for the biosynthesis of 2-alpha-glucosylglycerol.BIOCHEMICAL ENGINEERING JOURNAL,180,9. |
| MLA | Xu, Haichang,et al."@Robust enhancing stability and fructose tolerance of sucrose phosphorylase by immobilization on Ni-NTA functionalized agarose microspheres for the biosynthesis of 2-alpha-glucosylglycerol".BIOCHEMICAL ENGINEERING JOURNAL 180(2022):9. |
入库方式： OAI收割
来源：过程工程研究所
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