Jan 1, 1978

The influence of charged matrix surfaces on the thermostabilizing effect of calcium ions on immobilized fungal alpha-amylase

Acta biologica et medica Germanica
J FischerA Schellenberger

Abstract

The stabilizing effect of calcium ions on fungal alpha-amylase (EC 3.2.1.1) immobilized on a polystyrene anion exchanger (P+ amylase) was investigated and compared to the behaviour of soluble amylase. Moreover, gamma-(1,4-benzoquinone-2-yl)-aminopropyl silica-amylase (Si(n) amylase) as a conjugate with weakly basic amino groups and gamma-succinamidopropyl silica amylase (Si- amylase) as a conjugate with free carboxyl groups were applied for comparison. Depending on the calcium ion concentration the immobilized amylases showed a lower thermal stability than the soluble enzyme. The reduced stability was attributed to matrix effects in the microenvironment of the immobilized amylases and the calcium ion concentration in the carrier phase, which was changed in comparison with the external solution. Contrary to the non-measurable matrix effects in the microenvironment, altered calcium ion concentrations in the carrier phase of the polystyrene anion exchanger (P+) and gamma-succinamidopropyl silica (Si-) could be detected. With increasing calcium ion concentration a greater decrease of activity was observed for the soluble amylase than for the immobilized enzymes. The thermal stability of soluble amylase and P+ amylase was studied in...Continue Reading

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Mentioned in this Paper

Calcium
Calcium ion
1,4-benzoquinone
Salivary Amylase Measurement
Polystyrenes
Soluble
Non-Measurable Tumor Identification
Amylase Measurement
Hydrolase
Amylases

About this Paper

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