Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 4/17/2004
Publication Date: N/A
Citation: N/A Interpretive Summary:
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 become 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. However, once a new lipase has been found, another barrier for industrial utilization of lipases can be confronted, which is weak stability. One of the efficient ways to solve this problem is through immobilization of the enzyme since immobilization can increase the stability of the lipase in terms of temperature stability and also productivity. In this study, we investigated optimal reaction conditions for the immobilization of a novel lipase from Pichia lynferdii NRRL Y-7723 on hydrophobic resins. Environmental conditions tested included pH, temperature, incubation time, shaking speed, ratio of lipase over supporting material, and ionic strength. Of three hydrophobic resins tested, Phenyl-Sepharose showed the highest extent of immobilization with all reaction conditions tested. Butyl- and Octyl-Sepharose followed.