Isolation and Purification of Linoleate Isomerase from P. freudenreichii ssp. shermanii and L. plantarum

Using salting-out method, combined with Sephacryl S-200HR gel filtration chromatography and DEAE Sepharose F.F. ion exchange chromatography, linoleate isomerase was isolated and purified from P. freudenreichii ssp. shermanii and L. plantarum, respectively. linoleate isomerase from different sources showed different elution characteristics in the purification process. The molecular weight of linoleate isomerase from P. freudenreichii ssp. shermanii was 56 kDa, and that from L. plantarum was 50.65 kDa. The result indicated that big differences existed in the purification method of linoleate isomerase due to their different sources.