Purification and Partial Characterization of Esterase from Marine Vibrio fischeri
2009
P. Ranjitha | E.S. Karthy | A. Mohankumar
<p class="MsoNormal" style="margin: 0cm 0cm 4pt; line-height: 12pt; mso-line-height-rule: exactly; mso-pagination: widow-orphan;"><span style="font-size: 10pt; mso-font-kerning: 0pt; mso-fareast-language: EN-US;" lang="EN-US"><span style="font-family: Times New Roman;">Lipolytic enzymes from marine microbes have been the focus of intense and growing research. The bioluminescence bacterium <em style="mso-bidi-font-style: normal;">Vibrio fischeri</em> was produced esterase enzyme when the medium contained specific substrate. The esterase was purified from the concentrated culture supernatant. The most active fractions were obtained using the technique of precipitation with 1N HCl. The precipitated fraction was purified by ion exchange chromatography (DEAE-Cellulose) and gel filteration chromatography (Sephadex G200). The purified active fraction exhibiting final specific activity of 300U/mg and characterized; the optimum pH was 7.5, the optimum temperature was 30°C. The enzyme was very stable at the temperature 30°C and at wide range of pH. The enzyme was monomeric protein having molecular mass of 37 KDa estimated by native PAGE assay.</span></span></p>
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