Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification, Characterization and Application of a Cold Active Lipase from Marine Bacillus cereus HSS

  • Hassan, Sahar WM. (National Institute of Oceanography and Fisheries (NIOF)) ;
  • Abd El Latif, Hala H. (National Institute of Oceanography and Fisheries (NIOF)) ;
  • Beltagy, Ehab A. (National Institute of Oceanography and Fisheries (NIOF))
  • Received : 2021.09.10
  • Accepted : 2021.12.16
  • Published : 2022.03.28
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Abstract

Lipases (triacylglycerol acylhydrolases [EC 3.1.1.3]) are water-soluble enzymes. They catalyze the hydrolysis of fats and oils. A cold-active lipase from marine Bacillus cereus HSS, isolated from the Mediterranean Sea, Alexandria, Egypt, was purified and characterized. The total purification depending on lipase activity was 438.9 fold purification recording 632 U/mg protein. The molecular weight of the purified lipase was estimated to be 65 kDa using sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The optimum substrate concentration, enzyme concentration, pH, and temperature were 1.5 mM, 100 µl, pH 6 and 10℃, respectively. The lipase was tolerant to NaCl concentrations ranging from 1.5 to 4.5%. The lipase was affected by the tested metal ions, and its activity was inhibited by 16% in the presence of 0.05 M SDS. The application of the cold-active lipase for the removal of an oil stain from a white cotton cloth showed that it is a promising biological agent for the treatment of oily wastes and other related applications. To the best of our knowledge, this is the first report of the purification and characterization of a lipase from marine B. cereus HSS isolated from the Mediterranean Sea.

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References

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