Physiologie des Phenolabbaus bei <i>Rhodococcus</i> spec. P1 Teil 1: Beziehungen zwischen Wachstum und Phenolabbau

Hensel, Jürgen; Straube, G.

doi:10.1002/aheh.19830110606

Cited by 7 publications

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References 9 publications

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“…For subsequent enzymatic analysis the bacterial strain was cultivated with phenol in a standardized manner: 3-days-old agar slant cultures were inoculated into 100 ml of a synthetic medium (HENSEL and STRAUBE 1983) with 0.5 mg/ml phenol. After 6 h further 0.5 mg/ml, after 24 h and 32 h 1.0 mg/ml and after 48 h 0.05 mg/ml phenol were added.…”

mentioning

confidence: 99%

Phenol hydroxylase from Rhodococcus sp. P 1

Straube

1987

J. Basic Microbiol.

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mentioning

confidence: 99%

Phenol hydroxylase from Rhodococcus sp. P 1

Straube

1987

J. Basic Microbiol.

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Physiologie des Phenolabbaus bei Rhodococcus spec. P1. Teil 2: Untersuchungen zur Regulation des Phenolabbaus

Hensel

Straube

1984

Acta hydrochim. hydrobiol.

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Surrrmwy:The phenol-degrading system which can be induced in Rhodococcus spec. P 1 brings about the metabolization of phenol via the B-ketoadipate path (ortho-cleavage of caterhol).For the more precise characterization of the degradation performance investigations were made into the influences of different carbon sources: glucose, galactose, ribose, arabinose, xylose. aretate, citricacid, mandelic acid, protocatechoic acid, glycerol, tryptophane, phenylalanine and the complex substrate of nutrient broth as well as succinate, catechol and benzoate. Only the three last-named substances show an influence: succinate inhibits only the synthesis of phenol hydroxylase. catechol and benzoate inhibit the synthesis and activity of phenol hydroxylase. An a comparison of the results with literature shows, even a t the same path of degradation there are different regulating mechanismus in the different microorganisms. EinfiihrungFiir den aerohen Abbau von Phenol durch Mikroorganisrnen sind zwei Stoffwechselwege bekannt, die sich durch den Spaltungsmechanismus des Ringsystems und die Regulation der einzelnen Reaktionsschrit'te voneinander unterscheiden. Nach den1 Mechanismus der Ringspalt ung uird in ortho-Weg (0-Spaltung, /?-Ketoadipinsaure-Weg) und meta-Weg (m-Spaltung) unterteilt. Eine ganze Reihe von Arbeitsgruppen (GIBSON, KOCH and KALLIO; B.~YLY and DAGLEY;NEUJAHR et al. 1970 NEUJAHR et al. , 1973 NEUJAHR et al. , 1974 RIBBONS; SALA-TREPAT and EVANS; STANIER and ORNSTON; GIBSON; 11. a.) befaate sich mit der Aufklarung der nioglichen Abbauwege. Insgesamt fiihrten die Arbeiten zu folgender Vorstellung vom Phenolabbau (vgl. auch Abb. 1) : Als Zwischenprodukt wird stets Brenzkat,echin gebildet. Brenzkat,echin kann iin weit,eren Verlauf zwischen den Hydroxylgruppen oxydativ zur cis, cis-Muconsaure gespalten werden. Uber die Zwischenprodukte Muconolacton, Muconoenollacton und 8-Ketoadipinsaure werden schlieBlich die gut verwertbaren Metabolite Acetyl-CoA und Siiccinat gebildet. n'eben dieser ortho-Spaltung ist auch die iiieta-Spaltung des Brenzkatechins moglich. Dahei wird 2-Hydroxyinuconsaureseniialdehyd gebildet, fur den zwei Abbauniiiglichkeiten existieren, die zii Acetaldehyd und Pyruvat fuhren.

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Application of Exchangeable Biochemical Reactors with Oxidase‐Catalase‐Co‐immobilizates and Immobilized Microorganisms in a Microfluidic Chip‐Calorimeter

Leifheit¹,

Bergmann²,

Greiser³

2008

Engineering in Life Sciences

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Several methods for the quantitative detection of different compounds, e.g., L‐amino acids, sugars or alcohols in liquid media were developed by application of an automatic measuring unit including a fluid chip‐calorimeter FCC‐21. For this purpose, enzymes were immobilized covalently on the inner and outer surface of CPG (controlled porous glass)‐spherules with an outer diameter of 100 μm and filled into a micro flow‐through reaction chamber (VR = 20 μL). The design of the measuring cell allows for easy insertion into the calorimeter device of a stored series of comfortably pre‐fabricated measuring cells. These cells can be filled with different enzyme immobilizates. Different oxidases were used and co‐immobilized with catalase for the improvement of the detection sensitivity. A signal amplification could be achieved up to a factor of 3.5 with this configuration. β‐D‐glucose, ethanol and L‐lysine could be detected in a range of 0.25–1.75 mM using glucose oxidase, alcohol oxidase and lysine oxidase. The group of oxidases in combination with the enzymatic catalysis of the intermediate H2O2 allows the quantitative detection of a large number of analytes. A good measurement and storage stability could be achieved for several weeks by this immobilization method. In addition to enzyme‐based detection reactions, it was shown that living microorganisms can be immobilized in the reaction chamber. Thus, the system can be used as a whole‐cell biosensor. The quantitative detection of phenol in the range of 10–100 μM could be performed using the actinomycete Rhodococcus sp. immobilized on glass beads by means of embedding into polymers.

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Physiologie des Phenolabbaus bei Rhodococcus spec. P1 Teil 1: Beziehungen zwischen Wachstum und Phenolabbau

Abstract: Physiologie des Phenolabbaus bei

Cited by 7 publications

References 9 publications

Phenol hydroxylase from Rhodococcus sp. P 1

Phenol hydroxylase from Rhodococcus sp. P 1

Physiologie des Phenolabbaus bei Rhodococcus spec. P1. Teil 2: Untersuchungen zur Regulation des Phenolabbaus

Application of Exchangeable Biochemical Reactors with Oxidase‐Catalase‐Co‐immobilizates and Immobilized Microorganisms in a Microfluidic Chip‐Calorimeter

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