作者: Ichiro Chibata , Tetsuya Tosa , Tadashi Sato
DOI: 10.1128/AM.27.5.878-885.1974
关键词: Autolysis (biology) 、 Polyacrylamide gel electrophoresis 、 Ammonium fumarate 、 Enzyme 、 Bacteria 、 Escherichia coli 、 Chemistry 、 Aspartate ammonia-lyase 、 Metal ions in aqueous solution 、 Chromatography 、 General Pharmacology, Toxicology and Pharmaceutics 、 General Biochemistry, Genetics and Molecular Biology 、 General Immunology and Microbiology 、 General Medicine
摘要: The immobilization of asparatase-containing Escherichia coli was investigated by various methods, and the most active immobilized cells were obtained entrapment in a polyacrylamide gel lattice. Other bacteria also entrapped same method, enzymatically obtained. aspartase activity E. increased nine- to tenfold autolysis Enzymatic properties compared with those intact cells. optimal pH 8.5 for 10.5 activities not activated Mn(2+), which can activate native aspartases. heat stability somewhat higher than that Bivalent metal ions such as Mg(2+), Ca(2+) protected against thermal inactivation