Pseudomonas putida ATCC

A very efficient and universal method has been developed for the production of optically pue L- and D-amino adds. The prindple is based on the enantioselective hydrolysis of D,L-amino add amides. The stable D,L-amino add amides are effidently prepared under mild reaction conditions starting from simple raw materials (Figure A8.2). Thus reaction of an aldehyde with hydrogen cyanide in ammonia (Strecker reaction) gives rise to the formation of the amino nitrile. The aminonitrile is converted in a high yield to the D,L-amino add amide under alkaline conditions in the presence of a catalytic amount of acetone. The resolution step is accomplished with permeabilised whole cells of Pseudomonas putida ATCC 12633. A nearly 100% stereoselectivity in hydrolysing only the L-amino add amide is combined with a very broad substrate spedfidty. 

IJrocaninsaure aus Histidin (mit Achromobacter liquidum IAM 1667)3 l.-Asparaginsdure aus Ammoniumfumarat (mit Escherichia Coli ATCC 11 303)4 5 2 6 i.-Citridlin aus Arginin (mit Pseudomonas Putida ATCC 4359)7. 

Jones KH, RT Smith, PW Trudgill (1993) Diketocamphane enantiomer-specific Bayer-Villiger monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J Gen Microbiol 139 797-805. 

Microorganisms. A strain of Pseudomonas putida (ATCC, 17484 Med.-3 colony type) was cultured in 250-ml flasks containing 100 ml of the modified Fred-Waksman (9 ) medium. Flasks were inoculated from the stock culture and kept at room temperature for 3 days with continuous shaking. The bacterial cells were harvested by centrifugation at 6,000 g for 10 minutes. 

Biological. Four Pseudomonas sp., including Pseudomonas putida (ATCC culture 29607) isolated from soil, degraded chloropicrin by sequential reductive dechlorination. The proposed degradative pathway is chloropicrin -> nitrodichloromethane nitrochloromethane nitromethane + small amounts of carbon dioxide. In addition, a highly water soluble substance tentatively identified as a peptide was produced by a nonenzymatic mechanism (Castro et al., 1983). 

Boukhalfa H, Reilly SD, Michalczyk R, Iyer S, Neu P (2006) Iron (III) Coordination Properties of a Pyoverdin Siderophore Produced by Pseudomonas putida ATCC 33015. Inorg Chem 45 5607... 

Pseudomonas putida ATCC 11172 was used for both microbial calorimetry and for stripping phenol and lower cresols. Several isolates from local soils, which were able to combust larger aromatics such as cinnamic and syringic... 

P. C. Babbitt, J. A. Gerlt, G. L. Kenyon, Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633,... 

The aminopeptidase from Pseudomonas putida ATCC 12633 has also recently been cloned and overexpressed in E. coli resulting in a highly efficient whole-cell biocatalyst for industrial applications 1291. The specific activity of this new biocatalyst is substantially increased (25 times) compared with the specific activity of the P. putida wild type cells without changing the other positive characteristics of the aminopeptidase. Even though the aminopeptidase from Pseudomonas putida exhibits the relaxed substrate specificity described above, an a-hydrogen atom in the substrate is an essential structural feature for the enzymatic activity. Therefore this enzyme can not be used for the resolution of higher substituted amino acids. 

Diketocamphane 1,2-monooxygenase Pseudomonas putida ATCC 17453 2 2 identical substrate oxygenating subunits + NADH dehydrogenase NADH 78 (39 each) 1 FMN per subunit 7.2 [64]... 

Whilst the whole-cell approach has proved invaluable, the associated problems of overmetabolism and side reactions can be encountered. Another way to counter the problems of high cost in using isolated BVMOs is to use an NADH dependent enzyme, as NADH retails at approximately one tenth of the cost of NADPH. The Type 2 DKCMOs from Pseudomonas putida ATCC 17453 (= NCIMB 10007) are NADH dependent, and Grogan et al. were successftd in applying a complement of these enzymes, termed MOl, to the transformation of bicyclo[3.2.0]hept-2-en-6-one, to yield another enantiodivergent mix of lactones enantiomeric to those obtained... 

Figure 16.5-24. Biotransformation of bicyclo[3.2.0]hept-2-en-6-one by NADH dependent BVMOs from camphor grown Pseudomonas putida ATCC 17453.

The transformation of a series of norbomanone derivatives (Fig. 16.5-34) was studied by Roberts and coworkers who determined that both the MOl complement of NADH dependent BVMOs from Pseudomonas putida ATCC 17453 and the NADPH dependent fraction M02 were successful in the resolution of hydroxy, acetoxy and benzyloxy norbomanones11231. Interestingly 25DKCMO and 36DKCMO when separate, displayed notably different reactivity toward the hydroxy and acetoxy derivative, again emphasizing their complementary nature as potential individual biocatalysts. The benzyloxy lactone is an intermediate in the synthesis of the insect antifeedant azadirachtin. 

The ability of BVMOs to oxidize sulfur was also exploited by Beecher and Willetts in order to construct space filling cubic models of the active site of the DKCMO enzymes from Pseudomonas putida ATCC 17 453 (Fig. 16.5-40). They note that the more relaxed enantiospecificity of 36DKCMO, at least in terms of sulfoxidation, appears to be due to an overall larger 3D cubic space available in the active site11341. 36DKCMO appears to be the best candidate for a first X-ray structure of a BVMO, as preliminary crystal data have been reported1881. 

Benzaldehyde can be produced from benzoyl formate with whole cells of Pseudomonas putida ATCC 12633 as biocatalyst119 201 (Fig. 16.6-5). Alternatively, but less effectively, mandelic acid can be used as starting material. A pH of 5.4 was found to be optimal for benzaldehyde accumulation. At this proton concentration, partial inactivation of the benzaldehyde dehydrogenase isoenzymes and activation of the benzoyl formate decarboxylase are reported. Fed-batch cultivation prevented substrate inhibition. In situ product removal is necessary to prevent product inhibition. 

In the case of mcZ-PHAs, a Swiss group reports the continuous, growth-associated production of poly(3-hydroxyalkanoate-co-3-hydroxyalkenoates) in one-stage chemostat cultures of Pseudomonas putida ATCC 29147 in a single CSTR. The applied substrates encompassed 5-phenylvalerate, octanoate and 10-undecenoate. Multiple nutrient limited growth conditions were chosen at a dilution rate of D = 0.1 h . Different mixtures of the substrates in the feed resulted in the formation of copolyesters with varying compositions and different amounts of aromatic and unsaturated side chains that make the products accessible for further modification. Based on the results, the authors conclude that the steady state conditions in a continuous culture provide a strategy especially suited for the production of tailored PHA copolymers [117]. 

Phenol Cellulose acetate membranes Pseudomonas putida (ATCC 49451) Chung et a ., 1998... 

Phenol Activated carbon-filled cellulose acetate hollow-fiber membranes Pseudomonas putida ATCC 17484 Zhu et al., 2000... 

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