%A Anita Chaudhary
%A L.K. Gupta
%A J.K. Gupta
%A U C Banerjee
%O Copyright of this article belongs to Elsevier Science.
%J Journal of Biotechnology
%T Purification and properties of levanase from Rhodotorula sp.
%X 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 moleculer mass of the enzyme was 39 kDa. The purified levanase showed maximum activity at pH 6.0 and 40 ?C. Enzyme was quite stable at 4 ?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.
%N 1
%K Levanase; Purification; Chromatography; Rhodotorula sp
%P 55-61
%V 46
%D 1996
%I Elsevier Science
%R doi:10.1016/0168-1656(95)00183-2
%L open728