Carrageenan Immobilization of Glucose Isomerase
{'Code': '15030000', 'Directorate': {'Abbreviation': 'TIP', 'LongName': 'Dir for Tech, Innovation, & Partnerships'}, 'Division': {'Abbreviation': 'TI', 'LongName': 'Translational Impacts'}}
{'SignBlockName': 'Ritchie B. Coryell', 'PO_EMAI': None, 'PO_PHON': None}
Enzymes can be used as catalysts to make or modify products.                    Fructose syrup, a sweetener competitive with sucrose used in                    food, is produced by isomerization of glucose using an                          immobilized form of the enzyme glucose isomerase.  This                         represents the largest commercial application of an immobilized                 enzyme.  The PI plans to design and develop an improved                         immobilized form of glucose isomerase to produce pure fructose                  syrup that can be used directly in soft drinks.                                                                                                                 The criteria for measuring performance of an immobilized glucose                isomerase is its productivity in terms of total amount of                       fructose produced per unit of enzyme, determined by the combined                effects of stability and activity.  Activity and stability are                  very dependent upon both pH and temperature.  For continuous use                in fixed bed reactors, catalytic stability is the primary factor                in determining the practical productivity of immobilized enzymes.               The PI plans to design carrageenan-based supports for immobilized               enzymes which should increase productivity and yield.  The                      hypothesis is that carrageenan gels entrap the enzyme such that                 multiple sites on the gel interact with multiple sites on the                   surface of the enzyme by means of ionic bonds.  Under such                      conditions the multi-point attachment of enzymes to solid                       supports conditions the multi-point attachment of enzymes to                    solid supports makes the enzyme more rigid and thus less                        susceptible to unfolding.                                                                                                                                       This phase I work will involve:                                                                                                                                      (1)  Measuring the effects of pH and temperature on the                              stability and activity of the enzyme.                                                                                                                      (2)  Determining sensitivity of the enzyme to O2                                     inactivation and Ca++ inhibition.                                                                                                                          (3)  Measuring fructose yield under optimum conditions for                           productivity.                                                                                                                                         The staff and instrumentation are more than adequate and funding                is recommended.
{'FirstName': 'Robert', 'LastName': 'Henkens', 'PI_MID_INIT': 'W', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Robert W Henkens', 'EmailAddress': 'henkens@earthlink.net', 'PI_PHON': '2525047508', 'NSF_ID': '000404177', 'StartDate': '02/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Enzyme Technology Research Group Inc', 'CityName': 'Durham', 'ZipCode': '277012801', 'PhoneNumber': '9196833161', 'StreetAddress': '710 West Main Street', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'North Carolina', 'StateCode': 'NC', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'NC04', 'ORG_UEI_NUM': None, 'ORG_LGL_BUS_NAME': None, 'ORG_PRNT_UEI_NUM': None}
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{'Code': '5371', 'Text': 'SBIR Phase I'}
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