ISSN:
0138-4988
Schlagwort(e):
Life Sciences
;
Life Sciences (general)
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
Notizen:
Four silica supports differing in pore dimensions were activated by treatment with SiCl4 and then with ethylenediamine to obtain alkylamine groups on the silica surface. Three enzymes, peroxidase from cabbage, glucoamylase from Aspergillus niger C and urease from soybean were immobilized on these supports using glutaraldehyde as coupling agent. It was found that the protein content, the retained enzymatic activity and the storage stability of the silica supported enzymes were considerably affected by support pore size and enzyme molecular weight, the factors which are supposed to alter protein distribution inside the support pores. The highest activity was found for peroxidase and glucoamylase attached to the silica with the widest pores, but their loss in activity during storage was considerable. The urease retained less activity after immobilization, but its storage stability was excellent.
Zusätzliches Material:
5 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/abio.370090310
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