PURIFICATION AND PROPERTIES OF LEVANASE FROM RHODOTORULA SP

Levanase, a slime dissolving enzyme of Rhodotorula sp., was purified t o approx. 26-fold by ammonium sulphate precipitation, DEAE and gel fil tration (Sephacryl S-200) chromatography. The moleculer mass of the en zyme was 39 kDa. The purified levanase showed maximum activity at pH 6 .0 and 40 degrees C. Enzyme was quite stable at 4 degrees C and at pH 5.5 to 6.5. Hg2+ at a level of 10 mM completely inhibited the levanase activity, while 2-mercaptoethanol at the same concentration showed a 2.93-times increase in activity. In addition to levan, the enzyme also showed substrate specificity towards inulin.