Invertase immobilized on macroporous polystyrene: Properties and kinetic characterization

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Abstract
Invertase from baker's yeast (Saccharomyces cerevisiae) was covalently bound via benzoquinone and glutaraldehyde to a macroporous polystyrene anion exchanger. The behavior of the invertase–polystyrene complexes in batch and packed‐bed reactors was characterized kinetically. In addition to kinetic studies on sucrose hydrolysis at low initial substrate concentrations, the dependence of conversion degree on flow rate at high, industrially used substrate concentrations was determined. The described invertase–polystyrene complexes are suitable for technical application in the production of glucose–fructose mixtures because of their high specific and relative activities, as well as the good hydrodynamical and mechanical properties of the polystyrene matrix.