
A polyamide with the covalently coupled phosphatidyl ethanolamine was used for affinity adsorption of an alkaline lipase from Pseudomonas aeruginosa. The immobilization resulted in increase of the enzyme specific activity. Some properties of native and adsorbed enzyme were compared. The temperature optima, heat and pH stability, KM and Vmax values were determined for both native and immobilized enzymes.
Kinetics, Hydrolysis, Phosphatidylethanolamines, Pseudomonas aeruginosa, Temperature, Lipase, Hydrogen-Ion Concentration, Enzymes, Immobilized, Substrate Specificity
Kinetics, Hydrolysis, Phosphatidylethanolamines, Pseudomonas aeruginosa, Temperature, Lipase, Hydrogen-Ion Concentration, Enzymes, Immobilized, Substrate Specificity
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 0 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |
