[L-asparatic acid synthesis from ammonium fumarate by free and immobilized Escherichia coli cells].
E. coli 85 cells with a high aspartate-ammonia-lyase activity were immobilized through polyacrylamide gel incorporation. Proper conditions to assay aspartase activity of E. coli cells were developed. Kinetic patterns of aspartate-ammonia-lyase reaction catalyzed by free and immobilized E. coli 85 cells were studied. The synthesis of L-aspartic acid from ammonium fumarate had the following characteristics: specific activity of (4--6) . 10(-5) mmole/mg.sec for free cells and (6--8) . 10(-5) mmole/mg.sec for immobilized cells with their content in polyacrylamide gel of 5--10 mg protein per g wet gelm pH 8.3--10.0.
D001224:Aspartic Acid / Q000096:biosynthesis*; D004926:Escherichia coli / Q000378:metabolism*; D005650:Fumarates / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D000644:Quaternary Ammonium Compounds / Q000378:metabolism*; D013237:Stereoisomerism
D005650:Fumarates; D000644:Quaternary Ammonium Compounds; D001224:Aspartic Acid
Sintez L-asparaginovoĭ kisloty fumarata ammoniia svobodnymi i immobilizirovannymi kletkami Escherichia coli.