title: Mesoporous CLEAs-silica composite microparticles with high activity and enhanced stability.
abstract: A novel enzyme immobilization approach was used to generate mesoporous enzymes-silica composite microparticles by co-entrapping gelatinized starch and cross-linked phenylalanine ammonia lyase (PAL) aggregates (CLEAs) containing gelatinized starch into biomemitic silica and subsequently removing the starch by α-amylase treatment. During the preparation process, the gelatinzed starch served as a pore-forming agent to create pores in CLEAs and biomimetic silica. The resulting mesoporous CLEAs-silica composite microparticles exhibited higher activity and stability than native PAL, conventional CLEAs, and PAL encapsulated in biomimetic silica. Furthermore, the mesoporous CLEAs-silica composite microparticles displayed good reusability due to its suitable size and mechanical properties, and had excellent stability for storage. The superior catalytic performances were attributed to the combinational unique structure from the intra-cross-linking among enzyme aggregates and hard mesoporous silica shell, which not only decreased the enzyme-support negative interaction and mass-transfer limitations, but also improved the mechanical properties and monodispersity. This approach will be highly beneficial for preparing various bioactive mesoporous composites with excellent catalytic performance.
authors.affiliation: Research Center for Fermentation Engineering of Hebei, College of Bioscience and Bioengineering, Hebei University of Science and Technology, 26 Yuxiang Street, Shijiazhang 050018, P R China.|Tianjin Key Laboratory of Food-Biotechnology, Tianjin University of Commerce, Beichen district, Tianjin 300134, P R China.|Key Laboratory of Industry Microbiology, Ministry of Education, Tianjin University of Science and Technology, 29 Thirteenth Street, Tai Da Development Area, Tianjin 300457, P R China.
authors.forename: Jiandong
authors.initials: J
authors.lastname: Cui
authors.affiliation: Key Laboratory of Industry Microbiology, Ministry of Education, Tianjin University of Science and Technology, 29 Thirteenth Street, Tai Da Development Area, Tianjin 300457, P R China.
authors.forename: Shiru
authors.initials: S
authors.lastname: Jia
authors.affiliation: Research Center for Fermentation Engineering of Hebei, College of Bioscience and Bioengineering, Hebei University of Science and Technology, 26 Yuxiang Street, Shijiazhang 050018, P R China.
authors.forename: Longhao
authors.initials: L
authors.lastname: Liang
authors.affiliation: Research Center for Fermentation Engineering of Hebei, College of Bioscience and Bioengineering, Hebei University of Science and Technology, 26 Yuxiang Street, Shijiazhang 050018, P R China.
authors.forename: Yamin
authors.initials: Y
authors.lastname: Zhao
authors.affiliation: Research Center for Fermentation Engineering of Hebei, College of Bioscience and Bioengineering, Hebei University of Science and Technology, 26 Yuxiang Street, Shijiazhang 050018, P R China.
authors.forename: Yuxiao
authors.initials: Y
authors.lastname: Feng
mesh_terms: D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D007700:Kinetics; D053758:Nanoparticles / Q000737:chemistry / Q000648:ultrastructure; D010650:Phenylalanine Ammonia-Lyase / Q000378:metabolism; D016062:Porosity; D012822:Silicon Dioxide / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D010650:Phenylalanine Ammonia-Lyase