Burkholderia cepacia Pseudomonas

Mycobacterium sp. BBl Pseudomonas cepacia F297 Pseudomonas putida GZ44 Mycobacterium sp. RJGll-135 Burkholderia cepacia Pseudomonas paucimobilis Pseudomonas paucimobilis Mycobacterium vanbaalenii PYR-1... 

Less is known about the pathways of PAH degradation by co-cultures than about the pathways of degradation by individual bacteria and fungi (Juhasz Naidu, 2000). Four bacteria Pseudomonas aeruginosa, Pseudomonas cepacia (=Burkholderia cepacia). Pseudomonas sp. and Ralstonia pickettii) and four fungi (Alternaria tenuis, Aspergillus terreus, Trichoderma... 

With lipases, improved dyeing behavior, water absorption, and oil stain resistance of PET fabrics have been claimed following treatment with enzymes from T. insolens [1, 62, 72, 101] and T. lanuginosus [4, 11, 26]. Treatment of PET fabrics with lipases from Aspergillus spp., Beauveria brongniartii, C. antarctica, C. cylindracea, Rhizomucor miehei, Burkholderia cepacia. Pseudomonas fluores-cens, Rhizopus spp., and porcine (hog) pancreas lipase resulted in increased hydrophilicity, moisture regain, and water absorption values [4,33,38,44,51,52,60,103]. 

Burkholderia cepacia (Pseudomonas cepacia) 33 PDB2LIP Schrag et al. (1997)... 

Burkholderia cepacia has formerly been known as Pseudomonas cepacia. 

Burkholderia (formeriy Pseudomonas) cepacia is intrinsically resistant to a number of biocides, notably benzalkonium chloride and chlorhexidine. Again, the outer membrane is likely to act as a permeability barrier. By contrasL Ps. stutzeri (an organism implicated in eye infections caused by some cosmetic products) is invariably intrinsically sensitive to a range of biocides, including QACs and chlorhexidine. This organism contains less wall muramic acid than other pseudomonads but it is imclear as to whether this could be a contributory factor in its enhanced biocide susceptibility. 

Lipase ANL, lipase from Aspergillus niger, BCL, lipase from Burkholderia cepacia (formerly Pseudomonas cepacia) CAL-B, lipase from Candida antarctica B PPL, lipase from Pseudomonas fluorescens PPL, pig pancreatic lipase. 

Various cyclic esters have been subjected to hpase-catalyzed ring-opening polymerization. Lipase catalyzed the ring-opening polymerization of 4- to 17-membered non-substituted lactones.In 1993, it was first demonstrated that medium-size lactones, 8-valerolactone (8-VL, six-membered) and e-caprolactone (e-CL, seven-membered), were polymerized by lipases derived from Candida cylindracea, Burkholderia cepacia (lipase BC), Pseudomonas fluorescens (lipase PF), and porcine pancreas (PPL). °... 

Rhodococcus globerulus P6 Burkholderia cepacia LB 400 Pseudomonas pseudoalcaligenes KF 707 Pseudomonas sp. KKS 102 Sphingomonas paucimobilis SYK 6 Pseudomonas sp. CA 10 Escherichia coli C Escherichia coli Alcaligenes eutrophus IMP 222 Sphingomonas paucinwbilis SYK 6... 

The complexity introduced by exposure of an established mixed culture growing with a single substrate to an alternative cosubstrate is illustrated by the following. A stable mixed culture of Pseudomonas putida mt-2, P. putida FI, P. putida GJ31, and Burkholderia cepacia G4 growing with limited concentrations of toluene was established. Exposure to TCE for a month resulted in the loss of viability of the last three organisms, and resulted in a culture dominated by P. putida mt-2 from which mutants had fortuitously arisen (Mars et al. 1998). 

Scheme 1.20 Regioselective esterification of lobucavir (PCL Pseudomonas cepacia lipase, now known as Burkholderia cepacia)...

From Burkholderia cepacia (formerly Pseudomonas cepacia) three siderophores named omibactins (33) were isolated for which the stmctures were determined by... 

The stmcture of pyochelin (for a detailed bibliography, see (57)), a secondary siderophore of Pseudomonas aeruginosa and of Burkholderia cepacia was established (75) as 2-(2-o-hydroxyphenyl-2-thiazolin -yl)-3-methylthiazolidine-4-carboxylic acid. It consists of a mixture of two easily interconvertible stereoisomers (pyochelin I and II) differing in the configuration of C-2". They can be separated by chromatography, but in methanolic solution (not in DMSO) the equilibrium (ca. 3 1) is restored quickly. For a discussion of the mechanism of isomerization, see (57, 577). 

Meyer JM, Van VT, Stintzi A, Berge O, Winkehnann G (1995) Omibactin Production and Transport Properties in Strains of Burkholderia vietnamensis and Burkholderia cepacia (formerly Pseudomonas cepacia). BioMetals 8 309... 

Zamri A, Abdallah MA (2000) An Improved Stereocontrolled Synthesis of Pyochelin, Siderophore of Pseudomonas aeruginosa and Burkholderia cepacia. Tetrahedron 56 249... 

In addition to cutinases, various lipases, such as from C. antarctica, Candida sp. [13, 47], Thermomyces lanuginosus [2, 14, 15, 55, 56], Burkholderia (formerly Pseudomonas) cepacia [57] and esterases from Pseudomonas sp. (serine esterase) [58] and Bacillus sp. (nitrobenzyl esterases) [59, 60], have shown PET hydrolase... 

Although quite reliable empirical rules exist for the enantioselectivity of hydrolases for secondary alcohols (see Section 4.2.1.2), such rules are not as developed for primary alcohols, partly because many hydrolases often show low enantioselectivity. With some exceptions, lipases from Pseudomonas sp. and porcine pancreas lipase (PPL) often display sufficient selectivity for practical use. The model described in Figure 4.3 has been developed for Pseudomonas cepacia lipase (reclassified as Burkholderia cepacia), and, provided that no oxygen is attached to the stereogenic center, it works well for this lipase in many cases [41]. However, as soon as primary alcohols are resolved by enzyme catalysis, independent proof of configuration for a previously unknown product is recommended. 

Burkholderia cepacia (formerly Pseudomonas cepacia) TMP-SMZ Ceftazidime, chloramphenicol... 

An example for the application of enzymatic kinetic resolutions with high E values in natural product synthesis is the chemoenzymatic synthesis of the northern half of epothilones (also see Sect. 4.1). Various lipases and esterases could be found with outstanding enantioselectivity (up to >100) among these were lipase B from Candida antarctica, a lipase from Burkholderia cepacia, a lipase from Pseudomonas sp., and a lipase from Streptomyces diastochromogenes, all affording the desired (S)-configurated alcohol with >99% enantiomeric excess (Fig. 4) [65],... 

The natural products epothilone A and B are structurally different from taxol but have similar anticancer activity. Significantly, they have been reported to be much more active against cell lines exhibiting multiple-drug resistance [26], Taylor and co-workers at the University of Notre Dame have recently published an elegant, formal total synthesis of epothilone A [27], In this work, the authors used the CLC form of Burkholderia cepacia (formerly Pseudomonas cepacia) lipase (ChiroCLEC -PC) to resolve a key alcohol intermediate by selective acylation with vinyl acetate in /-butyl methyl ether (Fig. 6). The enantioselectivity was >20 1 at 47% conversion and efficiently provided gram quantities of the desired (R) alcohol. Since the unreacted (S) alcohol can easily be epimerized by a simple oxidation-reduction sequence and the catalyst reused without significant loss in activity, the method is ideally suited for scale-up. 

As increasing research has been carried out with these enzymes, a less empirical approach has been taken as a result of the different substrate profiles that have been compiled for various enzymes in this class. These profiles have been used to construct active site models for such versatile enzymes as the carboxylester hydrolase, pig liver esterase (PLE) (E.C. 3.1.1.1), and the microbial lipases (E.C. 3.1.1.3) from Burkholderia cepacia (formerly Pseudomonas cepacia) lipase (PCL), Candida... 

A general rule describing Burkholderia cepacia lipase (formerly called Pseudomonas cepacia lipase, PCL) catalysed conversions of primary alcohols with a chiral carbon in the / -position is depicted in Scheme 6.3. This rule, however, is only reliable if there are no oxygen substituents on the chiral carbon [14]. 

It is generally stated that biocatalysis in organic solvents refers to those systems in which the enzymes are suspended (or, sometimes, dissolved) in neat organic solvents in the presence of enough aqueous buffer (less than 5%) to ensure enzymatic activity. However, in the case of hydrolases water is also a substrate and it might be critical to find the water activity (a ) value to which the synthetic reaction (e.g. ester formation) can be optimized. Vahvety et al. [5] found that, in some cases, the activity of Candida rugosa lipase immobihzed on different supports showed the same activity profile versus o but a different absolute rate. With hpase from Burkholderia cepacia (lipase BC), previously known as lipase from Pseudomonas cepacia, and Candida antarctica lipase B (CALB) it was found that the enzyme activity profile versus o and even more the specific activity were dependent on the way the enzyme was freeze dried or immobihzed [6, 7]. A comparison of the transesterification activity of different forms of hpase BC or CALB can be observed in Tables 5.1 and 5.2, respectively. 

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