ARS | Publication request: IMMOBILIZATION AND HYPERACTIVATION 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 Only
Publication Acceptance Date: May 9, 2004
Publication Date: May 12, 2004
Citation: KIM, Y., LEE, G., KIM, I., LEE, K., HA, T., HOU, C.T., KIM, H. IMMOBILIZATION AND HYPERACTIVATION OF A NOVEL LIPASE FROM PICHIA LYNFERDII NRRL Y-7723. ANNUAL MEETING AND EXPO OF THE AMERICAN OIL CHEMISTS' SOCIETY. 2004.

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. Although lipases have been used for several years to modify the structure and composition of fats and oils, they have only recently become available for large-scale use in industry, mainly because of their high 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. However, once a new lipase has been found, another barrier for industrial utilization of lipase can be confronted, which is weak stability. One of the efficient ways to solve this problem is through immobilization, which can increase the stability of the lipase in terms of temperature and also productivity. In this study, we tried to find optimal environmental conditions for the immobilization of a novel lipase from Pichia lynferdii NRRL Y-7723 which we screened from 23 yeast extracellular lipases. Environmental conditions tested include pH, temperature, supporting material, incubation time, shaking speed, ratio of lipase/supporting material, and ionic strength. Thermal and pH stability of lipase after immobilization was also tested.