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.
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Thornton et al. (1975) studied this question.
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