Applied Biochemistry and Biotechnology

, Volume 113, Issue 1–3, pp 145–159 | Cite as

Screening of Dowex® anion-exchange resins for invertase immobilization

  • Ester Junko Tomotani
  • Michele VitoloEmail author


Commercial yeast invertase (Bioinvert®) was immobilized by adsorption on anion-exchange resins, collectively named Dowex® (1×8:50–400, 1×4:50–400, and 1×2:100–400). Optimal binding was obtained at pH 5.5 and 32°C. Among different polystyrene beads, the complex Dowex-1×4–200/invertase showed a yield coupling and an immobilization coefficient equal to 100%. The thermodynamic and kinetic parameters for sucrose hydrolysis for both soluble and insoluble enzyme were evaluated. The complex Dowex/invertase was stable without any desorption of enzyme from the support during the reaction, and it had thermodynamic parameters equal to the soluble form. The stability against pH presented by the soluble invertase was between 4.0 and 5.0, whereas for insoluble enzyme it was between 5.0 and 6.0. In both cases, the optimal pH values were found in the range of the stability interval. The K m and V max for the immobilized invertase were 38.2 mM and 0.0489 U/mL, and for the soluble enzyme were 40.3 mM and 0.0320 U/mL.

Index Entries

Invertase immobilization exchange resins Dowex® 


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Copyright information

© Humana Press Inc. 2004

Authors and Affiliations

  1. 1.Department of Biochemical and Pharmaceutical Technology, Pharmaceutical Sciences SchoolUniversity of São PauloSão Paulo, SPBrazil

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