Purification and Characterization of Laccase-1 from Pleurotus Florida
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Purification and Characterization of Laccase-1
from Pleurotus Florida
|
|
| Creator |
Das, N
Chakraborty, T K Mukherjee, M |
|
| Subject |
Drug Development/Diagnostics & Biotechnology
|
|
| Description |
Pleurotus florida (ITCC 3308) produces two
laccase enzymes (L 1 and L2) in potato-dextrose media containing
0.5 % yeast extract. Concentrated culture filtrate was separated
on DEAE-Sephadex (A-50) column into two enzyme
peaks, subsequently named L I and L 2. The L 1 enzyme has been
purified to homogeneity by ion-exchange and gel-permeation
chromatography L 1 is a monomeric glycoprotein with a molar
mass of 77 and 82 kDa as determined by SDS-PAGE and gelfiltration chromatography, respectively. The pl value of L 1 has
been determined to be 4.1. The optimum reaction temperature
of the enzyme is 50 ~ The K m and some other kinetic parameters
of L 1 have been determined. Cyanide and azide completely
inhibit the enzyme activity. The enzyme was fully active
in 1 : 1 (V/V) buffer-chloroform for at least 2 h. Spectroscopic
analysis revealed that the enzyme has four copper atoms,
a type 1 copper, a type 2 copper and a type 3 binuclear copper.
|
|
| Date |
2000
|
|
| Type |
Article
PeerReviewed |
|
| Format |
application/pdf
|
|
| Identifier |
http://www.eprints.iicb.res.in/821/1/FOLIA_MICROBIOLOGICA___45(_5)447%2D451;2000[69].pdf
Das, N and Chakraborty, T K and Mukherjee, M (2000) Purification and Characterization of Laccase-1 from Pleurotus Florida. Folia Microbiologica, 45 (5). pp. 447-451. |
|
| Relation |
http://dx.doi.org/10.1007/BF02817619
http://www.eprints.iicb.res.in/821/ |
|