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Purification and properties of levanase from Rhodotorula sp
A Chaudhary1, L K Gupta, J K Gupta
1Division of Environmental Sciences, IARI, New Delhi, India.
Journal of Biotechnology
|April 18, 1996
Abstract:
Levanase, a slime dissolving enzyme of Rhodotorula sp., was purified to approx. 26-fold by ammonium sulphate precipitation, DEAE and gel filtration (Sephacryl S-200) chromatography. The molecular mass of the enzyme 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.