Purification and Characterization of the Lipase from Marine Vibrio fischeri


  •  P. Ranjitha    
  •  E. Karthy    
  •  A. Mohankumar    

Abstract

Lipolytic enzymes from marine microbes have been the focus of intense and growing research. The bioluminescence
bacterium Vibrio fischeri was produced lipase enzyme when the medium contained specific substrate. The lipase was
purified from the concentrated culture supernatant. The most active fractions were obtained using the technique of
precipitation with ammonium sulphate. The precipitated fraction was purified by desalting and ion exchange
chromatography. The purified active fraction exhibiting final specific activity of 121U/mg and characterized; the
optimum pH was likely between 7 to 8, the optimum temperature was 30°C and about 80 % of activity at 5°C. The
enzyme was very stable at the pH 8, at the temperature 30°C. The enzyme was monomeric protein having molecular
mass of 57 KDa estimated by native PAGE assay.


This work is licensed under a Creative Commons Attribution 4.0 License.
  • Issn(Print): 1916-9671
  • Issn(Onlne): 1916-968X
  • Started: 2009
  • Frequency: quarterly

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