Purification and properties of levanase from Rhodotorula sp.

Chaudhary, Anita and Gupta, L.K. and Gupta, J.K. and Banerjee, U C (1996) Purification and properties of levanase from Rhodotorula sp. Journal of Biotechnology, 46 (1). pp. 55-61. ISSN 01681656

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Official URL: http://dx.doi.org/10.1016/0168-1656(95)00183-2


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.

Item Type: Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Uncontrolled Keywords: Levanase; Purification; Chromatography; Rhodotorula sp
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 27 Jan 2012 15:30
Last Modified: 28 Mar 2012 09:55
URI: http://crdd.osdd.net/open/id/eprint/728

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