A novel method for immobilization of invertase from the thermophilic fungus, Thermomyces lanuginosus

An invertase from the thermophilic fungus, Thermomyces lanuginosus was immobilized on phenyl-Sepharose and its properties were studied. Between the soluble and immobilized forms of the invertase, there were not much difference in their optimum pH, K _M and V _max for sucrose. In contrast, the K _M and V _max for raffinose changed significantly. The optimum temperature for the immobilized invertase was lower by 10 C. The immobilized invertase showed remarkable stability at 50 C and was less sensitive to inhibition by metal ions. There was no leaching of the enzyme for at least a month when stored in the refrigerator. The method is novel and specific for the thermophilic invertase as a mesophilic invertase (from yeast) did not bind to phenyl-Sepharose.