ISOLATION AND PROPERTIES OF RECOMBINANT INULINASES FROM <i>Aspergillus </i>sp.
The genes <i>inuA </i>and <i>inu1</i>, encoding two inulinases (32nd glycosyl hydrolase family) from <i>Aspergillus niger </i>and <i>A. awamori </i>heterologous fungus, were cloned into <i>Penicillium canescens </i>recombinant strain. Using chromatographic techniques endo-inulinase InuA (56 kDa, pI 3) and exo-inulinase Inu1 (60 kDa, pI 4.3) were purified to homogene- ity from the enzymatic complexes of <i>P. canescens </i>new transformants. The properties, such as substrate specificity, pH- and T-optima of activity, stability at different temperature conditions, the influence of the cations and anions on the catalytic activity etc. of both recombinant inulinases were studied