Purification and characterization of esterase from marine <i style="">Vibrio fischeri</i> isolated from squid
NOPR - NISCAIR Online Periodicals Repository
View Archive InfoField | Value | |
Title |
Purification and characterization of esterase from marine Vibrio fischeri isolated from squid
|
|
Creator |
Mohankumar, A
Ranjitha, P |
|
Subject |
Vibrio fischeri
Extracellular enzymes , Esterase RP-HPLC |
|
Description |
262-269
Bioluminescence bacterium Vibrio fischeri was produces esterase enzyme when the medium contained specific substrate. Esterase was purified from the culture supernatant. Most active fractions were obtained using the technique of precipitation with 1N HCl. Precipitated fraction was purified by ion exchange chromatography (DEAE-Cellulose) and gel filtration chromatography (Sephadex G200). Enzyme purity was determined by RP-HPLC. Purified active fraction exhibiting final specific activity of 300U/mg and characterized; the optimum pH was 7.5, the optimum temperature was 30°C. Enzyme was very stable at the temperature 30°C and at wide range of pH. Enzyme was monomeric protein having molecular mass of 37 kDa estimated by native PAGE assay. |
|
Date |
2010-07-29T11:11:58Z
2010-07-29T11:11:58Z 2010-06 |
|
Type |
Article
|
|
Identifier |
0975-1033 (Online); 0379-5136 (Print)
http://hdl.handle.net/123456789/10021 |
|
Language |
en_US
|
|
Publisher |
CSIR
|
|
Source |
IJMS Vol.39(2) [June 2010]
|
|