[Penicillin amidase from E. coli. Some physicochemical properties of the enzyme incorporated into polyacrylamide gel].
The physico-chemical properties of penicillinamidase (PA) immobilized in polyacrylamide gel (IPA) were investigated. It was shown that simple incorporation of PA into polyacrylamide gel was not effective because of gradual washing out of the enzyme. The use of a complex method for the immobilization (immobilization in the presence of a linking agent) resulted in higher stability of IPA, the choice of the optimal ratio of the reagents being of paramount importance. The mechanical strength of IPA was studied in model experiments.
D000178:Acrylamides / Q000494:pharmacology*; D000581:Amidohydrolases / Q000494:pharmacology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004355:Drug Stability; D004800:Enzymes, Immobilized; D004926:Escherichia coli / Q000201:enzymology*; D005782:Gels; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010316:Particle Size; D010399:Penicillin Amidase / Q000494:pharmacology*; D011485:Protein Binding; D013535:Suspensions; D013997:Time Factors
D000178:Acrylamides; D004800:Enzymes, Immobilized; D005782:Gels; D013535:Suspensions; D000581:Amidohydrolases; D010399:Penicillin Amidase
Penitsillinamidaza iz E. coli. Nekotorye fiziko-khimicheskie svoĭstva fermenta, vkliuchennogo v poliakrilamidnyĭ gel'