ARS | Publication request: PRODUCTION OF A NOVEL LIPASE FROM PICHIA LYNFERDII NRRL Y-7723

Submitted to: Annual Meeting and Expo of the American Oil Chemists' Society
Publication Type: Abstract
Publication Acceptance Date: May 9, 2003
Publication Date: N/A

Technical Abstract: Lipases hydrolyze or synthesize triglycerides with positional and substrate specificities. The reactions catalyzed by lipases include hydrolysis, glycerolysis, esterification, acidolysis, and interesterification. In recent years, interest in the use of enzymes as hydrolytic or synthetic chiral catalysts has risen rapidly. However, although lipases have been used for several years to modify the structure and composition of fats and oils, they only recently became available for large-scale use in industry, mainly because of the high enzyme cost and appropriate selectivity for industrial purposes. In this regard, industry continues to look for economical sources of lipases with high activity and characteristic selectivity. In this study, we screened 16 yeast extracellular lipases and found a novel highly active lipase from Pichia lynferdii NRRL Y-7723. P. lynferdii produced a hundred-fold more extracellular lipase than other yeast strains tested. Lipase was produced by growing cultures on nutritional medium in the presence of 1% soybean oil at 25 deg for 86 hours. Among several well-known nutritional carbon and nitrogen sources, sucrose and yeast extract were characterized as the best carbon and nitrogen sources, respectively, for highest lipase production. Optimal concentrations of yeast extract and sucrose were 15 g/L and 10 g/L, respectively. Optimal concentrations of soybean oil and initial medium pH for lipase production were 3% and pH 5~6, respectively. In addition to the fermentation variables mentioned above, several other important factors influencing lipase production were studied.