Preparation of L (+) beta-hydroxyisobutyric acid by bacterial oxidation of isobutyric acid

A process for the bacterial oxidation of isobutyric acid to L(+) β-hydroxyisobutyric acid has been developed. The strain of Pseudomonas putida (ATCC 21244) used in this fermentation was isolated from local soil. The process was carried out in a 15-liter fermentor over a period of 70 hr and produced L(+) β-hydroxyisobutyric acid in conversions as high as 48%. Hydroxylation of the methyl group of isobutyric acid has special interest because it is difficult to perform chemically. The useful chemical syntheses of β-hydroxyisobutyric acid available at present do not start with isobutyric acid and are not stereospecific.     

Conferences and symposia sponsored by the Aquatic Ecosystem Health and Management Society

Conferences and symposia sponsored by the Aquatic Ecosystem Health and Management Society     

Kinetic and electrophoretic characterization of NADP dependent dehydrogenases from root tissues of Norway spruce [Picea abies (L.) Karst.] employing a rapid one-step extraction procedure

Summary The NADPH generating enzymes glucose-6-phosphate dehydrogenase (EC 1.1.1.49), 6-phosphogluconate dehydrogenase (EC 1.1.1.44), and isocitrate-dehydrogenase (NADP dependent; EC 1.1.1.42) have been characterized in spruce [Picea abies (L.) Karst.] roots. Interference from inherent phenolic compounds was minimized by complexation with borate and insoluble polyvinylpyrrolidone in the presence of 2-mercaptoethanol and NADP. A further addition of protective substances had no (bovine serum albumin) or even an inhibitory effect (ascorbate) on the enzyme activities. The enzymes were shown to be strictly NADP specific. The optimal pH values and the apparent Michaelis constants from spruce roots are in good agreement with data from different photosynthetic organisms and gametophytic tissues of conifers. Native electrophoresis and subsequent activity staining showed the same banding patterns for enzymes both from root and needle tissues. In addition, the applicability of a highly sensitive dot-blot assay for the accurate quantification of the extracted protein is shown.