Microbial degradation of secondaryn-alkyl sulfates and secondary alkanols

Lijmbach, G. W. M.; Brinkhuis, Elisabeth

doi:10.1007/bf02578884

Cited by 27 publications

(9 citation statements)

References 9 publications

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“…Microorganisms grow at the expense of primary and secondary alkyl sulphates (Payne 1963;Payne & Feisal 1963;Lijmbach & Brinkhuis 1973). These alkyl sulphates are initially degraded by the removal of the sulphate group (Payne et al 1965;Dodgson & White 1983).…”

Section: Alkyl Sulphatesmentioning

confidence: 99%

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Complete degradation of xenobiotic surfactants by consortia of aerobic microorganisms

Ginkel

1996

Biodegradation

163

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Linear alkylbenzene sulphonates are primarily attacked via a hydroxylation of the alkyl chain from the methyl group followed by beta-oxidation. The alkyl chain is metabolized by pure cultures to give sulphophenyl carboxylates which accumulate in the medium. In mixed culture, other microorganisms are capable of degrading sulphophenyl carboxylates. Formation of ethylene glycol monosulphates as major products of alkyl ethoxy sulphates demonstrates that the ether bonds are cleaved. The bacteria involved in growing on the alkyl chain are unable to utilize the hydrophilic moiety. This hydrophilic moiety, in turn, is degraded by other microorganisms. The degradation of alkylphenol ethoxylates and highly branched alcohol ethoxylates proceeds by shortening the polyoxyethylene chain leaving the hydrophobic part of the molecule. The biodegradation of linear alcohol ethoxylates and ethoxylated fatty amines is initiated by a central cleavage or omega-oxidation. Subsequent oxidation of the alkyl chains results in the production of polyethylene glycols and secondary ethoxylated amines. Both polar moieties are metabolized by other microorganisms. Degradation of alkyltrimethylammonium salts and alkylamines is initiated by a cleavage of the Calkyl-N bond. The central fission leads to the formation of alkanals which are readily converted by beta-oxidation. The alkyl chain-utilizing bacteria are not able to degrade the methylamines. The methylamines, in turn, are subject to biodegradation by methylotrophs. The limited metabolic capacities of pure cultures of microorganisms utilizing surfactants point to the requirement of consortia to degrade surfactants completely. Complete degradation of surfactants is accomplished by mixed cultures of microorganisms constructed on the basis of synergistic and commensalistic relationships. However, degradation of a surfactant by one member of a commensalistic consortium may lead to the production of toxic or non-toxic metabolites. Waste water treatment without the build up of such metabolites can be achieved in plants operated with sludge retention times that are suitable for maintaining all microorganisms of the consortium. In contrast, in natural ecosystems the introduction of a surfactant may result in a transient formation of a metabolite.

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Section: Alkyl Sulphatesmentioning

confidence: 99%

“…The alkanone undergoes hydroxylation at the carbon adjacent to the carbonyl group, followed by oxidation to the dione. Hydrolysis of the dione generates an alkanoic acid and alkanal suitable for/3-oxidation (Lijmbach & Brinkhuis 1973).…”

Section: Alkyl Sulphatesmentioning

confidence: 99%

Complete degradation of xenobiotic surfactants by consortia of aerobic microorganisms

Ginkel

1996

Biodegradation

163

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“…Other work on a different Pseudomonas species has shown that secondary alkyl sulphates can be completely oxidized to CO2, H20 and sulphate. Enzymic desulphation apparently precedes the initial oxidation of the liberated secondary alcohol to the corresponding ketone (Lijmbach & Brinkhuis, 1973). Comamonas terrigena, a co-isolate of Pseudomonas C 12B, can also degrade some secondary alkyl sulphates and has been shown to produce two alkylsulphohydrolases.…”

mentioning

confidence: 99%

Preliminary observations on alcohol dehydrogenases in Comamonas terrigena that exhibit stereospecificity towards secondary alcohols

Barrett¹,

Dodgson²,

White³

et al. 1980

Biochemical Journal

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Extracts of the cells of Comamonas terrigena, grown under a variety of different conditions, contain two distinct, constitutive, NAD-dependent alcohol dehydrogenase enzymes that can be separated by polyacrylamide-gel electrophoresis. One of the enzymes exhibits activity towards D-alkan-2-ols and primary alcohols and the other is active towards L-alkan-2-ols, symmetrical secondary alcohols and probably other positional isomers of secondary alcohols of the L-configuration. Methods for the individual assay of the two enzymes have been developed and have been used to define some of their general properties. Most of the substrates for these enzymes would not support growth of C. terrigena under the experimental conditions used and were relatively poorly oxidized by resting cell suspensions.

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“…Biodegradation of primary and secondary alkyl sulphate detergents by soil micro-organisms requires the initial removal of the sulphate group by primary and secondary alkylsulphohydrolases, and this is followed by the oxidation of the liberated alcohol (Williams & Payne, 1964;Payne et al, 1967;Lijmbach & Brinkhuis, 1973). Efforts in these laboratories have focused on the alkylsulphohydrolases present in two soil micro-organisms, Pseudomonas C12B and Comamonas terrigena.…”

mentioning

confidence: 99%

Substrate specificity and other properties of the inducible S3 secondary alkylsulphohydrolase purified from the detergent-degrading bacterium Pseudomonas C12B

Shaw¹,

Dodgson²,

White³

1980

Biochemical Journal

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The inducible S3 secondary alkylsulphohydrolase of the soil bacterium Pseudomonas C 12B was purified to homogeneity (683-fold from cell-free extracts by a combination of column chromatography on DEAE-cellulose, Sephadex G-100 and Blue Sepharose CL-6B. The enzyme has a molecular weight in the region of 40000-46 000, and is active over a broad range of pH from 5 to 9, with maximum activity at pH 8.2. The preferred substrates of the enzyme are the symmetrical secondary alkylsulphate esters such as heptan-4-yl sulphate and nonan-5-yl sulphate and the asymmetric secondary octyl and nonyl sulphate esters with the sulphate group attached to C-3 or C-4. However, for each asymmetric ester, the L-isomer is much more readily hydrolysed than the D-isomer. This specificity is interpreted in terms of a three-point attachment of the substrate to the enzyme's active site. The alkyl chains on either side of the esterified carbon atom are bound in two separate sites, one of which can only accommodate alkyl chains of limited size. The third site binds the sulphate group. Enzymic hydrolysis of this group is accompanied by complete inversion of configuration at the asymmetric carbon atom. The implied cleavage of the C-O bond of the C-O-S ester linkage was confirmed by 180-incorporation studies.

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Microbial degradation of secondaryn-alkyl sulfates and secondary alkanols

Cited by 27 publications

References 9 publications

Complete degradation of xenobiotic surfactants by consortia of aerobic microorganisms

Complete degradation of xenobiotic surfactants by consortia of aerobic microorganisms

Preliminary observations on alcohol dehydrogenases in Comamonas terrigena that exhibit stereospecificity towards secondary alcohols

Substrate specificity and other properties of the inducible S3 secondary alkylsulphohydrolase purified from the detergent-degrading bacterium Pseudomonas C12B

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