ICAR Research Data Repository for Knowledge Management
Purification and properties of levanase from Rhodotorula sp.
DIR@IMTECH: CSIR-Institute of Microbial Technology
View Archive Info| Field | Value | |
| Title |
Purification and properties of levanase from Rhodotorula sp.
|
|
| Creator |
Chaudhary, Anita
Gupta, L.K. Gupta, J.K. 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
PeerReviewed |
|
| Format |
application/pdf
|
|
| Identifier |
http://crdd.osdd.net/open/728/1/banejee1996.pdf
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://dx.doi.org/10.1016/0168-1656(95)00183-2
http://crdd.osdd.net/open/728/ |
|