Immobilization of β-glucuronidase in lysozyme-induced biosilica particles to improve its stability  

作　　者：Xiaokai SONG Zhongyi JIANG Lin LI Hong WU 

机构地区：[1]Key Laboratory for Green Chemical Technology of Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China [2]Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin 300072, China

出　　处：《Frontiers of Chemical Science and Engineering》2014年第3期353-361,共9页化学科学与工程前沿（英文版）

摘　　要：Mesoporous silica particles were prepared for efficient immobilization of the β-glucuronidase （GUS） through a biomimetic mineralization process, in which the solution containing lysozyme and GUS were added into the prehydrolyzed tetraethoxysilane （TEOS） solution. The silica particles were formed in a way of biomineralization under the catalysis of lysozyme and GUS was immobilized into the silica particles simultaneously during the precipitation process. The average diameter of the silica particles is about 200 nm with a pore size of about 4 rim. All the enzyme molecules are tightly entrapped inside the biosilica nanoparticles without any leaching even under a high ionic strength condition. The immobilized GUS exhibits significantly higher thermal and pH stability as well as the storage and recycling stability compared with GUS in free form. No loss in the enzyme activity of the immobilized GUS was found after 30-day＇s storage, and the initial activity could be well retained after 12 repeated cycles.Mesoporous silica particles were prepared for efficient immobilization of the β-glucuronidase （GUS） through a biomimetic mineralization process, in which the solution containing lysozyme and GUS were added into the prehydrolyzed tetraethoxysilane （TEOS） solution. The silica particles were formed in a way of biomineralization under the catalysis of lysozyme and GUS was immobilized into the silica particles simultaneously during the precipitation process. The average diameter of the silica particles is about 200 nm with a pore size of about 4 rim. All the enzyme molecules are tightly entrapped inside the biosilica nanoparticles without any leaching even under a high ionic strength condition. The immobilized GUS exhibits significantly higher thermal and pH stability as well as the storage and recycling stability compared with GUS in free form. No loss in the enzyme activity of the immobilized GUS was found after 30-day＇s storage, and the initial activity could be well retained after 12 repeated cycles.

关 键 词：silica nanoparticles BIOCATALYSIS biomimeticsynthesis β-glucuronidase encapsulation storage andrecycling stability 

分 类 号：TS202.3[轻工技术与工程—食品科学] TF124[轻工技术与工程—食品科学与工程]