Lipase Mediated Interesterification of Triglycerides
{'Code': '07020000', 'Directorate': {'Abbreviation': 'ENG', 'LongName': 'Directorate For Engineering'}, 'Division': {'Abbreviation': 'CBET', 'LongName': 'Div Of Chem, Bioeng, Env, & Transp Sys'}}
{'SignBlockName': 'Dov Jaron', 'PO_EMAI': None, 'PO_PHON': None}
Research into the catalytic modification of triglycerides by                    lipolytic enzymes is underway.  The objective is to clearly                     delineate the enzymatic action of lipases on lipid substrates in                systems with minimal water content.  Experiments will be                        conducted on the interesterification of two model triglycerides,                tripalmitin, and triolein, a specific example of a reaction                     involving lipid modification by lipases.  The experiments will                  examine and compare two alternate modes of substrate-enzyme                     contact (a) through enzymic reaction in organic solvents, and (b)               through enzymic reaction in biphasic reversed micellar solutions.               The studies will be directed to determine conditions for optimal                lipase activity in essentially non-aqueous systems, with                        maintenance of a high selectivity to interesterification over                   hydrolysis.  The role of organic solvents, the effects of water                 content and buffer ionic strength, colipase effects, substrate                  specificities, and cation levels are various system parameters to               be considered.  A thermodynamic framework for optimal solvent                   design and selection will be developed, based on modified                       solubility parameter criteria.  Recent developments in gas                      chromatography will be applied involving heat-stable capillary                  columns and on-column injection techniques, to facilitate rapid                 analyses of triglyceride mixtures.                                                                                                                              Liapases have traditionally been recognized for their ability to                break down triglycerides through hydrolysis.  They have,                        therefore, been studied extensively for their medical relevance                 to atheroschlerosis and their industrial relevance to the                       production of long chain fatty acids from vegetable oils.  It is                only in recent years that their ability to function effectively                 in low water content systems has been recognized.  Under such                   conditions, lipase action is one of lipid synthesis and                         modification, rather than lipid breakdown.  Tremendous                          possibilities exist for lipase catalyzed biomodification and                    biosynthesis of several oleochemicals of importance to the                      pharmaceutical, food, and specialty chemicals industries.  The                  synthesis of esters for example, has applications to the                        production of biocompatible surfactants that are important as                   emulsifiers in food, cosmetics, and pharmaceuticals. The                        interesterification reaction, the focus of the present research,                involves fatty acid interchange between two triglycerides and has               direct application to the production of high value edible oils,                 such as cocoa butter substitutes.  The understanding of lipase                  action in lipid modification is still limited; it is the                        objective to further this understanding through a comprehensive                 study of a specific reaction.  Long term directions for the                     research on lipases will focus on applying the fundamental                      knowledge acquired through this project to a variety of novel                   reactions involving lipid modification and synthesis.
{'FirstName': 'Vijay', 'LastName': 'John', 'PI_MID_INIT': 'T', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Vijay T John', 'EmailAddress': 'vijay.john@tulane.edu', 'NSF_ID': '000206852', 'StartDate': '04/15/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Tulane University', 'CityName': 'NEW ORLEANS', 'ZipCode': '701185665', 'PhoneNumber': '5048654000', 'StreetAddress': '6823 SAINT CHARLES AVE', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Louisiana', 'StateCode': 'LA', 'CONGRESSDISTRICT': '01', 'CONGRESS_DISTRICT_ORG': 'LA01', 'ORG_UEI_NUM': 'XNY5ULPU8EN6', 'ORG_LGL_BUS_NAME': 'ADMINISTRATORS OF THE TULANE EDUCATIONAL FUND, THE', 'ORG_PRNT_UEI_NUM': 'XNY5ULPU8EN6'}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '140200', 'Text': 'BIOCHEMICAL & BIOMASS ENG'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8721829.xml'}