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@Robust enhancing stability and fructose tolerance of sucrose phosphorylase by immobilization on Ni-NTA functionalized agarose microspheres for the biosynthesis of 2-alpha-glucosylglycerol
Xu, Haichang1,2; Wei, Bin1,2; Liu, Xiaojie1,2; Huang, Yongdong3; Zhou, Weiqing3,4; Liang, Hao1,2
2022-03-01
Source PublicationBIOCHEMICAL ENGINEERING JOURNAL
ISSN1369-703X
Volume180Pages:9
AbstractSucrose 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.
KeywordSucrose phosphorylase Immobilization Agarose Stability Fructose tolerance
DOI10.1016/j.bej.2022.108362
Language英语
WOS KeywordSECONDARY STRUCTURE ; ENZYME ; GLUCOSYLGLYCEROL ; NANOPARTICLES ; RAMAN
Funding ProjectNational 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 Research AreaBiotechnology & Applied Microbiology ; Engineering
WOS SubjectBiotechnology & Applied Microbiology ; Engineering, Chemical
Funding OrganizationNational Key Research and Development Program of China ; National Natural Science Foundation of China ; Hebei Key Research and Development Project
WOS IDWOS:000760987100001
PublisherELSEVIER
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/52171
Collection中国科学院过程工程研究所
Corresponding AuthorZhou, Weiqing; Liang, Hao
Affiliation1.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
Recommended Citation
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.
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