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Title: REGIOSELECTIVITY OF NEW BACTERIAL LIPASES DETERMINED BY HYDROLYSIS OF TRIOLEIN

Author
item Lanser, Alan
item Manthey, Linda
item Hou, Ching

Submitted to: Current Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 8/27/2001
Publication Date: 2/1/2002
Citation: LANSER, A.C., MANTHEY, L.K., HOU, C.T. REGIOSELECTIVITY OF NEW BACTERIAL LIPASES DETERMINED BY HYDROLYSIS OF TRIOLEIN. CURRENT MICROBIOLOGY. 2002. V. 44. P. 336-340.

Interpretive Summary: Lipases are enzymes found in plants and animals. Their best known function is to break down fats. Under certain conditions, however, these enzymes can also build fat molecules, either from scratch, or by rearranging fat components. Not all lipases do this in the same manner and some are more active than others. In addition to being used to analyze fats after breakdown, lipases are being tested for use in the food, pharmaceutical, detergents and personal care product industries. Intense research is being done to produce specialty fats for diets for infants and adults. Only a few lipases have been developed for commercial use and these are costly. This study examines bacteria as a new, inexpensive lipase source, the method of fat breakdown, and differences found in those tested.

Technical Abstract: The newly identified lipases of 67 bacterial strains from the ARS Culture Collection, primarily Bacillus and Pseudomonas, have been characterized based on their positional specificity for triglycerides (triolein). Lipase was produced by growing the cultures in tryptone-glucose-yeast extract medium for 24 hr at 30 degrees C before addition of triglyceride. The lipase was allowed to act on the triglyceride for three days before analysis by thin layer chromatography. Of the bacterial lipases tested, fifty-five displayed random specificity, nine were 1,3 specific, and three showed no apparent lipase activity under these conditions.