Abstract
The suitability of hornblende as a support for immobilized β-fructofuranosidase (invertase) was studied, with regard to the physical stability of the support and the thermal and operational stability of the immobilized enzyme. Hornblende was more stable than Enzacryl-Alo or Enzacryl-TIO, and marginally more stable than porous glass. Invertase immobilized on hornblende was more stable during long-term operation than invertase immobilized on porous glass. An active preparation of immobilized invertase was obtained also on pyroxene particles.
| Original language | English (Ireland) |
|---|---|
| Pages (from-to) | 1679-1693 |
| Journal | Biotechnology and Bioengineering |
| Volume | 17 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Nov 1975 |
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