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Immobilization of penicillin G acylase on non-porous ultrafine silica particles

Fazelinia, H ; Sharif University of Technology | 2005

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  1. Type of Document: Article
  2. Publisher: Sharif University of Technology , 2005
  3. Abstract:
  4. In this paper, immobilization of penicillin G aclylase onto non-porous ultrafine silica particles has been studied. The amount of penicillin G acylase immobilized was increased by increasing the free enzyme concentration and, at 0.45 mg/ml concentration of the free enzyme, 80% of the enzyme was immobilized. The optimum pH for immobilization was found to be 7.0, close to the pl of the enzyme. Although immobilization of the enzyme on ultrafine silica particles with and without glutaraldehyde showed almost the same activities, the enzyme immobilized with glutaraldehyde retained its initial activity much longer during 40 cycle-repeated batches with a half life of 163.2 h. © Sharif University of Technology
  5. Keywords:
  6. Adsorption ; Biotechnology ; Composition effects ; Crosslinking ; Hydrolysis ; Mass transfer ; Microorganisms ; Particles (particulate matter) ; pH effects ; Proteins ; Silica ; Free enzyme concentration ; Glutaraldehyde ; Non-porous ultrafine silica particles ; Penicillin acylase ; Enzyme immobilization ; pharmaceutical industry
  7. Source: Scientia Iranica ; Volume 12, Issue 3 , 2005 , Pages 295-299 ; 10263098 (ISSN)
  8. URL: http://scientiairanica.sharif.edu/article_2496.html