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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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 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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