Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supports
✍ Scribed by A. Flynn; D. B. Johnson
- Publisher
- John Wiley and Sons
- Year
- 1978
- Tongue
- English
- Weight
- 451 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
Abstract
Glucoamylase from four different companies was studied: three had similar stability (half‐life at 50°C about 140 hr); the fourth was less stable (half‐life at 50°C about 20 hr). The immobilized enzymes were all less stable than their soluble counterparts: immobilized enzyme stability depended on the soluble enzyme used, the support, and method of immobilization. Thus enzyme bound to Enzacryl‐TIO was less stable than enzyme bound to hornblende (metal‐link method); this, in turn, was less stable than enzyme bound to hornblende by a silane–glutaraldehyde process. Bound enzyme stability was also improved by the presence of substrate or product (starch maltose or glucose). After 110 hr at 50°C in the presence of maltose (10% (w/v)) one preparation (a more stable soluble enzyme boul1d to hornblende by a silane–glutaraldehyde process) retained over 95% of its activity: activity loss was too low to permit the estimation of a half‐life.