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Application of chitosan-entrapped β-galactosidase in a packed-bed reactor system

Wentworth, Danielle S. ; Skonberg, Denise ; Donahue, Darrell W. ; Ghanem, Amyl

Journal of applied polymer science, 2004-01, Vol.91 (2), p.1294-1299 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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  • Título:
    Application of chitosan-entrapped β-galactosidase in a packed-bed reactor system
  • Autor: Wentworth, Danielle S. ; Skonberg, Denise ; Donahue, Darrell W. ; Ghanem, Amyl
  • Assuntos: Applied sciences ; biopolymers ; crosslinking ; enzymes ; Exact sciences and technology ; hydrolytic activity ; packed-bed reactor ; Physicochemistry of polymers ; Polymer industry, paints, wood ; Technology of polymers
  • É parte de: Journal of applied polymer science, 2004-01, Vol.91 (2), p.1294-1299
  • Notas: ArticleID:APP13276
    istex:89991FE1B62704CE4FC3DEA2ADB349074098C93B
    ark:/67375/WNG-0LSSRVX9-T
  • Descrição: The model enzyme β‐galactosidase was entrapped in chitosan gel beads and tested for hydrolytic activity and its potential for application in a packed‐bed reactor. The chitosan beads had an enzyme entrapment efficiency of 59% and retained 56% of the enzyme activity of the free enzyme. The Michaelis constant (Km) was 0.0086 and 0.011 μmol/mL for the free and immobilized enzymes, respectively. The maximum velocity of the reaction (Vmax) was 285.7 and 55.25 μmol mL−1 min−1 for the free and immobilized enzymes, respectively. In pH stability tests, the immobilized enzyme exhibited a greater range of pH stability and shifted to include a more acidic pH optimum, compared to that of the free enzyme. A 2.54 × 16.51‐cm tubular reactor was constructed to hold 300 mL of chitosan‐immobilized enzyme. A full‐factorial test design was implemented to test the effect of substrate flow (20 and 100 mL/min), concentration (0.0015 and 0.003M), and repeated use of the test bed on efficiency of the system. Parameters were analyzed using repeated‐measures analysis of variance. Flow (p < 0.05) and concentration (p < 0.05) significantly affected substrate conversion, as did the interaction progressing from Run 1 to Run 2 on a bed (p < 0.05). Reactor stability tests indicated that the packed‐bed reactor continued to convert substrate for more than 12 h with a minimal reduction in conversion efficiency. © 2003 Wiley Periodicals, Inc. J Appl Polym Sci 91: 1294–1299, 2004
  • Editor: Hoboken: Wiley Subscription Services, Inc., A Wiley Company
  • Idioma: Inglês
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