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    STUDIA BIOLOGIA - Issue no. 1 / 2019  
         
  Article:   PRODUCTION AND CHARACTERIZATION OF HALOPHILIC ESTERASE AND LIPASE FROM HALOPHILIC MICROORGANISMS .

Authors:  TEPPEI ISHIKAWA, HIROAKI MINEGISHI, YASUHIRO SHIMANE. 		 
       
         
  Abstract:   Lipase belongs to the hydrolases and is also known as fat-splitting enzyme, glycerol ester hydrolase or triacylglycerol acylhydrolase. Lipase catalyzes the hydrolysis of triglycerides converting them to glycerol and fatty acids. These are widely used in many industrial fields such as oil and fat processing, fabrication of soap, detergent, chemicals, food, pharmaceuticals, and so on. Halophilic enzymes can be highly active not only under high salinity but also in organic solvents and under high temperature. Therefore, in this study, we aimed to look for novel haloarcheal lipase capable of maintaining enzyme activity even under high salt concentration, at high temperature and in organic solvent enviroments. Ninety-seven strains producing lipase were isolated from the 668 different kinds of commercial salt samples. Results of the 16S rRNA gene sequences analysis of two isolates having high lipase activity especially have indicated that they are closely related to Pseudomonas halophila and Halospina denitrificans, respectively. They produced clear zones around colonies on agar plates containing 1.0% Tween 80. Optimal activities of crude enzymes from halophilic isolates were at 50-60oC, pH 8.0-9.0, and 20% (w/v) NaCl. Furtheremore, high activity and stability over broad ranges of temperature (40-70oC), pH (7.0-10.0) and NaCl concentration (15-30%) were observed, showing thermostable and halostable properties of the lipases produced by isolated strains.

Keywords: fatty ester, halophilic lipase, halophilic microorganism, lipid. 		 
         
     
         
         
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