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Purification and characterization of esterase from marine <i style="">Vibrio fischeri</i> isolated from squid

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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]