ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260171110