title: [Adsorption immobilization of alkaline lipase].
abstract: 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.
authors.forename: E Ia
authors.initials: EIa
authors.lastname: Sof'ina
authors.forename: M M
authors.initials: MM
authors.lastname: Rakhimov
authors.forename: I V
authors.initials: IV
authors.lastname: Shteĭn
authors.forename: I M
authors.initials: IM
authors.lastname: Arends
authors.forename: V V
authors.initials: VV
authors.lastname: Dorokhov
mesh_terms: D004800:Enzymes, Immobilized; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D010714:Phosphatidylethanolamines / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D010714:Phosphatidylethanolamines; D008049:Lipase
vernacular_title: Adsorbtsionnaia immobilizatsiia shchelochnoĭ lipazy.