Isolation and Identification of Styrene-degrading<i>Corynebacterium</i>Strains, and Their Styrene Metabolism

Yoshida, Kiyoshi; Okada, Keisaku

doi:10.1271/bbb.60.1826

Cited by 60 publications

(42 citation statements)

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“…Recently, the catabolism of aromatic compounds by Pseudomonas putida strain KT2440 has been reviewed at the genomic level 22) . Nevertheless, some Grampositive bacteria, such as members of the genera Corynebacterium, Rhodococcus and Streptomyces, are able to mineralize a wide array of aromatic compounds 2,13,15,19,20,28,34) . Comparative studies indicated that there are extensive differences between the biodegradation processes in Grampositive and Gram-negative bacteria 3,9,12,14,16,19,25,27) .…”

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“…Several Corynebacterium species isolated from soil are able to degrade styrenes 20) , 2,4-dichlorobenzoate 28) , 2,4,6-trinitrotoluene 14) or other aromatic compounds 5,7,10,34) . Our previous studies demonstrated that C. glutamicum could use different aromatic compounds as a sole source of carbon and energy and, multiple ring cleavage pathways might occur in this bacterium [31][32][33] .…”

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Genomic Analysis and Identification of Catabolic Pathways for Aromatic Compounds in Corynebacterium glutamicum

2005

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The catabolism of aromatic compounds in Corynebacterium glutamicum was investigated by genome data mining and by experimental analysis. Results indicated that C. glutamicum assimilated different aromatic compounds such as phenol, p-cresol, benzoate, 4-hydroxybenzoate, vanillate, vanillin, resorcinol, 3,5-dihydroxytoluene and 2,4-dihydroxybenzoate. Genome data indicated, and enzyme assays confirmed; the existence of multiple ring-cleavage pathways for the catabolism of central aromatic intermediates; the protocatechuate and catechol branches of the -ketoadipate pathway, two similar hydroxyquinol pathways and the gentisate pathway. Two putative hydroxyquinol 1,2-dioxygenase genes (ncg11113 and ncg12951) were cloned and functionally identified in Escherichia coli. The genes encoding enzymes for the conversion of phenol, benzoate, 3-hydroxybenzoate, 4-hydroxybenzoate and vanillate in the central -ketoadipate pathways were mapped on the chromosome of C. glutamicum. A unique 30-kb (approximately 1% of the entire genome) catabolic island that channels the degradation of various aromatic compounds was mapped to position 2525-2555 kb of the genome. The global analysis and characterization of aromatic degradation pathways provided new insights into the metabolic ability of C. glutamicum in addition to its well-known ability to produce various amino acids and vitamins.

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Genomic Analysis and Identification of Catabolic Pathways for Aromatic Compounds in Corynebacterium glutamicum

2005

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“…Therefore, we performed the screening of a novel enzyme reducing PTK to (S)-PTE by using 2-propanol as a hydrogen donor, which would have the opposite stereoselectivity to PAR. A screening strategy was used to investigate microorganisms grown on gaseous styrene because, under such selective conditions, the microorganisms isolated from soil would be restricted to certain coryneform bacteria and Pseudomonas (9), in which useful ADHs have already been reported (2,8).…”

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Purification and Characterization of a Novel Alcohol Dehydrogenase from Leifsonia sp. Strain S749: a Promising Biocatalyst for an Asymmetric Hydrogen Transfer Bioreduction

Inoue

Makino

Itoh

2005

Appl Environ Microbiol

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To find microorganisms that could reduce phenyl trifluoromethyl ketone (PTK) to (S)-1-phenyltrifluoroethanol [(S)-PTE], styrene-assimilating bacteria (ca. 900 strains) isolated from soil samples were screened. We found that Leifsonia sp. strain S749 was the most suitable strain for the conversion of PTK to (S)-PTE in the presence of 2-propanol as a hydrogen donor. The enzyme corresponding to the reaction was purified homogeneity, characterized and designated Leifsonia alcohol dehydrogenase (LSADH). The purified enzyme had a molecular weight of 110,000 and was composed of four identical subunits (molecular weight, 26,000). LSADH required NADH as a cofactor, showed little activity with NADPH, and reduced a wide variety of aldehydes and ketones. LSADH catalyzed the enantioselective reduction of some ketones with high enantiomeric excesses (e.e.): PTK to (S)-PTE (>99% e.e.), acetophenone to (R)-1-phenylethanol (99% e.e.), and 2-heptanone to (R)-2-heptanol (>99% e.e.) in the presence of 2-propanol without an additional NADH regeneration system. Therefore, it would be a useful biocatalyst.

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“…The fatty acid content was also analyzed by NCIMB Japan, and a monounsaturated normal chain composition was detected. Although these are typical properties of Rhodococcus erythropolis, a deficiency of glucose utilization was also observed (11). Thus, we concluded that this microorganism should be identified as Rhodococcus sp.…”

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confidence: 73%

Engineering of Phenylacetaldehyde Reductase for Efficient Substrate Conversion in Concentrated 2-Propanol

Makino

Inoue

Dairi

2005

Appl Environ Microbiol

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Phenylacetaldehyde reductase (PAR) is suitable for the conversion of various aryl ketones and 2-alkanones to corresponding chiral alcohols. 2-Propanol acts as a substrate solvent and hydrogen donor of coupled cofactor regeneration during the conversion of substrates catalyzed by PAR. To improve the conversion efficiency in high concentrations of substrate and 2-propanol, selection of a PAR mutant library and the subsequent rearrangement of mutations were attempted. With only a single selection round and following the manual combination of advantageous mutations, PAR was successfully adapted for the conversion of high concentrations of substrate with concentrated 2-propanol. This method will be widely applicable for the engineering of enzymes potentially valuable for industry.The demand for enzymes in the chemical industry has expanded rapidly. Most enzymes can catalyze reactions at room temperature in a mild aqueous solution and have great substrate, stereo-, regio-, and chemoselectivity (12,15,16). Such properties are ideal for fine chemical production, particularly as chiral drug intermediates and agrochemicals.Alcohol dehydrogenase (ADH) (EC 1.1.1.1) can catalyze the asymmetric reduction of aldehyde or ketone to chiral alcohols. Phenylacetaldehyde reductase (PAR) from styrene-assimilating bacteria Rhodococcus sp. (formerly identified as Corynebacterium sp.) ST-10 belongs to the family of zinc-containing medium-chain ADHs (8). PAR has broad substrate specificity and catalyzes asymmetric reduction at high enantioselectivity in an NADH-dependent manner (8-10).Various examples of ADH applications for asymmetric reduction have been reported that use a cofactor regeneration system with additional enzymes such as formate dehydrogenase or glucose dehydrogenase (15). Recent reports have used the advantage of ADHs for NADH self regeneration with secondary alcohols as hydrogen donors (13, 21). We previously reported the ability of PAR to reduce various carbonyl compounds coupled with NADH self regeneration in the presence of 2-propanol as a proton donor (8). 2-Propanol can also profitably act as a solvent for the PAR substrates that cannot dissolve in aqueous media. However, at high concentrations of 2-propanol, the efficiency of substrate conversion by PAR clearly fell. Consequently, the conversion yields with high substrate concentrations were relatively low and insufficient for industrial application.Here, we attempted to engineer PAR that can operate in relatively high concentrations of 2-propanol (Ͼ20% [vol/vol]) to achieve efficient conversion of concentrated substrates without altering the substrate specificity. Using our method with the combination of advantageous mutations, PAR was successfully improved with six amino acid replacements with significant enhancement of the substrate conversion. Although relative yield of conversion at high concentration of 2-propanol was enhanced, little change of substrate specificity was observed. MATERIALS AND METHODSMaterials. All chemicals were of reagent grade. Taq DNA poly...

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Isolation and Identification of Styrene-degradingCorynebacteriumStrains, and Their Styrene Metabolism

Cited by 60 publications

References 2 publications

Genomic Analysis and Identification of Catabolic Pathways for Aromatic Compounds in Corynebacterium glutamicum

Genomic Analysis and Identification of Catabolic Pathways for Aromatic Compounds in Corynebacterium glutamicum

Purification and Characterization of a Novel Alcohol Dehydrogenase from Leifsonia sp. Strain S749: a Promising Biocatalyst for an Asymmetric Hydrogen Transfer Bioreduction

Engineering of Phenylacetaldehyde Reductase for Efficient Substrate Conversion in Concentrated 2-Propanol

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