title: Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particles.
abstract: Direct encapsulation of esterase or lipase fused with the silica-precipitating R5 peptide from Cylindrotheca fusiformis in silica particles afforded high yields of active entrapped protein. The hydrolytic activity of both enzymes against p-nitrophenyl butyrate was similarly affected by encapsulation and the enantioselectivity of the esterase was both improved and inverted.
authors.affiliation: Ingénierie des Systèmes Biologiques et des Procédés, Université de Toulouse, INSA, UPS, INP, 135 Avenue de Rangueil, F-31077 Toulouse, France.
authors.forename: Stéphane
authors.initials: S
authors.lastname: Emond
authors.forename: David
authors.initials: D
authors.lastname: Guieysse
authors.forename: Severine
authors.initials: S
authors.lastname: Lechevallier
authors.forename: Jeannette
authors.initials: J
authors.lastname: Dexpert-Ghys
authors.forename: Pierre
authors.initials: P
authors.lastname: Monsan
authors.forename: Magali
authors.initials: M
authors.lastname: Remaud-Siméon
mesh_terms: D000595:Amino Acid Sequence; D040761:Biomimetic Materials / Q000737:chemistry; D032701:Biomimetics; D011232:Chemical Precipitation; D017377:Diatoms / Q000737:chemistry / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D004950:Esterases / Q000737:chemistry / Q000378:metabolism*; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*
chemical_list: D004800:Enzymes, Immobilized; D010455:Peptides; D012822:Silicon Dioxide; D004950:Esterases; D008049:Lipase