[Comparison of the aspartase activity and its stability in Escherichia coli cells immobilized on polyacrylamide gel and carrageenan].
The conditions for immobilization of Escherichia coli cells (Soviet strain 85) on the natural polysaccharide carrier carrageenan (Soviet-made) were investigated and kinetic regularities of the aspartase reaction catalysed by immobilized in carrageenan cells of E. coli 85 were established. The conditions for retaining a high aspartase activity and stability of biocatalysts based on the E. coli 85 cells immobilized in PAAG and carrageenan were determined using full-loaded tanks for continuous synthesis of L-aspartic acid. The time-stable aspartase activity of the biocatalyst can be increased by treating the beads of the catalyst with bifunctional reagents (hexamethylenediamine, glutaraldehyde), the most active catalyst for the biotechnological synthesis of L-aspartic acid being obtained when carrageenan is used.
D000180:Acrylic Resins / Q000494:pharmacology*; D000642:Ammonia-Lyases / Q000378:metabolism*; D001220:Aspartate Ammonia-Lyase / Q000378:metabolism*; D001224:Aspartic Acid / Q000096:biosynthesis; D002351:Carrageenan / Q000494:pharmacology*; D002384:Catalysis; D004355:Drug Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D005782:Gels; D007700:Kinetics; D013696:Temperature
D000180:Acrylic Resins; D004800:Enzymes, Immobilized; D005782:Gels; C016680:polyacrylamide gels; D001224:Aspartic Acid; D002351:Carrageenan; D000642:Ammonia-Lyases; D001220:Aspartate Ammonia-Lyase
Sravnenie aspartaznoĭ aktivinosti i ee stabil'nosti u kletok Escherichia coli, immobilizovannykh v poliakrilamidnyĭ gel' i karraginan.