Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particles. Emond, S., Guieysse, D., Lechevallier, S., Dexpert-Ghys, J., Monsan, P., & Remaud-Simeon, M. Chemical Communications, 48(9):1314--1316, 2012.
doi  abstract   bibtex   
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.
@article{ emond_alteration_2012,
  title = {Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particles},
  volume = {48},
  issn = {1359-7345},
  doi = {10.1039/c1cc14478b},
  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.},
  language = {English},
  number = {9},
  journal = {Chemical Communications},
  author = {Emond, Stephane and Guieysse, David and Lechevallier, Severine and Dexpert-Ghys, Jeannette and Monsan, Pierre and Remaud-Simeon, Magali},
  year = {2012},
  keywords = {biosilica, expression system, immobilization, lipase, proteins, support, yarrowia-lipolytica},
  pages = {1314--1316}
}
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