A COMPARISON OF PROPERTIES OF INULINASES OF FUSARIUM-OXYSPORUM IMMOBILIZED ON VARIOUS SUPPORTS

Extracellular inulinase was obtained after growing Fusarium oxysporum for 9 days on a medium containing an aqueous extract of Cichorium inty bus roots. After partial purification, inulinase was immobilised by cr oss-linking it with water insoluble protein supports prepared from flo ur of soybean and mungbean, and egg white. Inulinase was also immobili sed by adsorbing it on DEAE-cellulose. Inulinase immobilised on soybea n and mungbean supports had a higher optimum temperature of 45-degrees -C as compared to 37-degrees-C of the free enzymes. Inulinase adsorbed on DEAE-cellulose was thermally the most stable whereas the inulinase cross-linked on soybean support was the least stable. Inulinase immob ilised on DEAE-cellulose and on supports obtained from mungbean and so ybean had a pH optima of 5.5, 6.5 and 6.0, respectively. The K(m) valu es of various immobilised inulinases with inulin varied from 0.25 to 0 .44 mmol dm-3.