Optimierung von Kulturbedingungen für <i>Acinetobacter calcoaceticus</i> beim Wachstum auf <i>n</i>‐Alkanen in einem Laborfermentor

The NADP+-dependent aldehyde dehydrogenase of Acinetobacter calcoaceticus was inducible by alkanes. It was located in the membranes surrounding the intracellular alkane inclusions. The enzyme could not be solubilized by changing of the p H or the ionic strength but by detergents a t concentrations around the critical micelle concentration. High concentrations of detergents inactivated the enzyme; reactivation was possible by addition of natural membrane phospholipids. The enzyme in intact membranes gave lower K m values than the enzyme in the micelle form. The size of the particles of cell envelopes (including the inclusion membranes) and of micelles was controlled by measurements of the wavelength dependence of turbidity. Proteinases were unable to solubilize the enzyme; in the presence of detergent they inactivated i t irreversibly. Phospholipase A, and D inactivated the enzyme reversibly.Die NADP-abhangige Aldehyddehydrogenase, induzierbar durch Alkane und Alkanole (AURICH u. EITNER 1977) Es wird angenonimen, daS das Enzyiu in einer Cardiolipin-Domane dieser Menibranen sitzen soll.In der ersten Mitteilung beschreiben wir den EinfluS von Detergentien, Proteinasen und Phospholipasen auf die Solubilisierung des Enzyins und seine Aktivitat. I n der zweiten Mitteilung sind unsere Ergebnisse uber die Rekonstitution des gereinigten Knzyms in kiinstlichen Meiiibranvesikeln (Liposomen) zusanlmengefafit (AURICH et aE. 1985).

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Wechselwirkungen der Aldehyddehydrogenase aus Acinetobacter calcoaceticus mit Membranlipiden I. Einfluß von Detergentien, Proteinasen und Phospholipasen auf die Solubilisierung und Aktivität des Enzyms

Aurich

Sorger

Bergmann

et al. 1985

J. Basic Microbiol.

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Wechselwirkungen der Aldehyddehdyrogenase aus Acinetobacter calcoaceticus mit Membranlipiden II. Rekonstitution in künstlichen Membranvesikeln

Aurich

Bergmann

Lasch

et al. 1985

J. Basic Microbiol.

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Purified aldehyde dehydrogenase (NADP+-dependent) of intracytoplasmic membranes of Acinetobacter cakcoaceticus could he incorporated from micelles formed during the purification procedure into liposomal membranes. Both the cholate dilution method and the ultrasonication method were suitable to produce enzyme liposomes. In unilamellar liposomes produced by phosphntidyl choline, the enzyme activity decreased to 1% (or less) of the original activity. In contrast, about 10% of the original activity could be preserved in unilamellar liposomes prepared from bacterinl phospholipids.The destruction of the enzyme liposomes induced by detergents (lauroyl sarcosinate) was followed by measuring the wavelength dependence of turbidity, which allowed us to draw conclusions on size and stability of the particles in the suspension. I n addition these measurements demonstrated that decanal and NADP+ did not destroy the liposomal structure a t concentrations necessary for the determination of enzyme activity.The liposomal enzyme was inactivated to a lesser degree by proteinase K than the micellar enzyme. Both phospholipase A, and D inactivated the enzyme incorporated into the liposomal membranes to about 50%. After t,reatment with phospholipase A,, the enzyme could be reactivated by bacterial phospholipids. After treatment with phospholipase D, no reactivation was possible by bacterial phospholipids.Die NADP-abhangige Aldehyddehydrogenase ist bei A . calcoaceticus ein Enzyin des Oxidations-Pathways der Alkane (AURICH u. EITNER 1977, SORGER u. AURICH 1978 und in den intracytoplasmatischen Umhiillungsmenibranen der Alkan-Inklusionen lokalisiert (VOAISEK et al. 1982). Sie liiljt sich durch Detergentien, wie Desoxycholat, Cholat, Laurylsarkosin und Triton X-100 solubilisieren (AURICH et al. 1985) und als Detergens-Phospholipid-Mischmizelle isolieren und reinigen . Wahrscheinlich ist Cardiolipin fur die Aktivitat des Enzynis essentiell (BERGMANN 1982

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Ultracytochemical localization of aldehyde dehydrogenase in Acinetobacter calcoaceticus

Sorger

Aurich

Fricke

et al. 1986

J. Basic Microbiol.

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A membrane-bound aldehyde dehydrogenase is induced in Acinetobacter calcoaceticus grown on aliphatic hydrocarbons as sole carbon source. This enzyme is NADP-dependent and is able to oxidize medium- and long-chain aliphatic aldehydes to their corresponding fatty acids. Electron micrographs of sectioned alkane-adapted bacteria showed hydrocarbon inclusions in the cytoplasmic matrix. The cytochemical phenazine methosulphate-tetranitro tetrazolium blue capture reaction allowed to localize the activity of the aldehyde dehydrogenase near the surface of these inclusions. At the same location we also found a NADPH tetrazolium-reducing activity.

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Optimierung von Kulturbedingungen für Acinetobacter calcoaceticus beim Wachstum auf n‐Alkanen in einem Laborfermentor

Cited by 6 publications

References 13 publications

Wechselwirkungen der Aldehyddehydrogenase aus Acinetobacter calcoaceticus mit Membranlipiden I. Einfluß von Detergentien, Proteinasen und Phospholipasen auf die Solubilisierung und Aktivität des Enzyms

Wechselwirkungen der Aldehyddehydrogenase aus Acinetobacter calcoaceticus mit Membranlipiden I. Einfluß von Detergentien, Proteinasen und Phospholipasen auf die Solubilisierung und Aktivität des Enzyms

Wechselwirkungen der Aldehyddehdyrogenase aus Acinetobacter calcoaceticus mit Membranlipiden II. Rekonstitution in künstlichen Membranvesikeln

Ultracytochemical localization of aldehyde dehydrogenase in Acinetobacter calcoaceticus

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