title: Purification and properties of levanase from Rhodotorula sp.
creator: Chaudhary, Anita
creator: Gupta, L.K.
creator: Gupta, J.K.
creator: Banerjee, U C
subject: QR Microbiology
description: 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.
publisher: Elsevier Science
date: 1996
type: Article
type: PeerReviewed
format: application/pdf
identifier: http://crdd.osdd.net/open/728/1/banejee1996.pdf
relation: http://dx.doi.org/10.1016/0168-1656(95)00183-2
identifier:   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     
relation: http://crdd.osdd.net/open/728/