Purification and properties of levanase from Rhodotorula sp.
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.
Chaudhary
A
A
Division of Environmental Sciences, IARI, New Delhi, India.
Gupta
L K
LK
Gupta
J K
JK
Banerjee
U C
UC
D000645:Ammonium Sulfate; D001426:Bacterial Proteins; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D002850:Chromatography, Gel / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008970:Molecular Weight; D012248:Rhodotorula / Q000201:enzymology*; D013816:Thermodynamics; D014462:Ultrafiltration / Q000379:methods
D001426:Bacterial Proteins; D006026:Glycoside Hydrolases; C021512:levanase; D000645:Ammonium Sulfate