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Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A study was undertaken to compare beta-glucuronidase-positive Escherichia coli counts produced by the ISO-GRID hydrophobic grid membrane filter method using SD-39 agar (test method) with those produced by AOAC Official Method 990.11, an existing ISO-GRID method using lactose monensin glucuronate agar and buffered MUG agar (reference method). The methods were evaluated using 21 food products, with three independent lots of five replicate samples analyzed per product by both methods. The test and reference methods were statistically equivalent for 19 of the 21 products; frozen, raw ground lamb produced significantly higher counts using the reference method, whereas counts obtained from cottage cheese were significantly higher using the SD-39 agar-based method.
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PMID:Enumeration of beta-glucuronidase-positive Escherichia coli in foods by using the ISO-GRID method with SD-39 agar. 967 81

The genetics of lactose utilization within the slow-lactose-fermenting Lactococcus lactis strain NCDO2054 was studied with respect to the organization, expression, and evolution of the lac genes. Initially the beta-galactosidase gene (lacZ) was cloned by complementation of an Escherichia coli mutant on a 7-kb HpaI fragment. Nucleotide sequence analysis of the complete fragment revealed part of a gal-lac operon, and the genes were characterized by inactivation and complementation analyses and in vitro enzyme activity measurements. The gene order is galK-galT-lacA-lacZ-galE; the gal genes encode enzymes of the Leloir pathway for galactose metabolism, and lacA encodes a galactoside acetyltransferase. The galT and galE genes of L. lactis LM0230 (a lactose plasmid-cured derivative of the fast-lactose-fermenting L. lactis C2) were highly similar at the nucleotide sequence level to their counterparts in strain NCDO2054 and, furthermore, had the same gene order except for the presence of the intervening lacA-lacZ strain NCDO2054. Analysis of mRNA for the gal and lac genes revealed an unusual transcriptional organization for the operon, with a surprisingly large number of transcriptional units. The regulation of the lac genes was further investigated by using fusions consisting of putative promoter fragments and the promoterless beta-glucuronidase gene (gusA) from E. coli, which identified three lactose-inducible intergenic promoters in the gal-lac operon. The greater similarity of the lacA and lacZ genes to homologs in gram-negative organisms than to those of gram-positive bacteria, in contrast to the homologies of the gal genes, suggests that the genes within the gal operon of L. lactis NCDO2054 have been recently acquired. Thus, the lacA-lacZ genes appear to have engaged the promoters of the gal operon in order to direct and control their expression.
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PMID:Transcriptional regulation and evolution of lactose genes in the galactose-lactose operon of Lactococcus lactis NCDO2054. 973 93

Most commercially available test kits for water and foodstuffs use beta-galactosidase activity for coliforms and beta-glucuronidase activity for Escherichia coli. We tested the effects on the beta-glucuronidase activity of E. coli W3110 of substances usually present in foods and several synthetic pharmaceutical compounds. Thirteen substances were tested: three carbohydrates, four flavonoids, five monosaccharide derivatives, and dimethyl sulphoxide. In a minimum medium without any other carbon source, glucose (0.1 mM), quercetin (0.1 mM), silymarin (10 mg/L), D-gluconic acid (0.01 mM), D-gluconic acid lactone (0.01 mM), isopropyl-beta-D-thiogalacto pyranoside (1 mM), p-nitrophenyl beta-D-glucuronide (1 mM), and DMSO (1 M) completely inhibited E. coli glucuronidase activity at the above concentrations. However, the following compounds stimulated E. coli glucuronidase activity within the ranges of concentrations shown: glucose (0.0001-0.01 mM), lactose and sucrose (>0.1 mM), D-saccharic acid 1,4 lactone (0.0001-0.1 mM), p-nitrophenyl beta-D-glucuronide (0.001-0.01 mM) and DMSO (2-500 mM). In a rich culture medium that contained other carbon sources (lauryl tryptose broth) E. coli glucuronidase activity in the presence of the extra nutrients was unaffected by the test substances and therefore, under normal conditions in water or foods, they should not interfere with E. coli assays based on measurements of beta-glucuronidase activity.
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PMID:Interference by carbohydrate substrates, flavonoids, and monosaccharide derivatives on bacterial beta-D-glucuronidase assays. 977 76

The lactose operon from Lactobacillus casei is regulated by very tight glucose repression and substrate induction mechanisms, which made it a tempting candidate system for the expression of foreign genes or metabolic engineering. An integrative vector was constructed, allowing stable gene insertion in the chromosomal lactose operon of L. casei. This vector was based on the nonreplicative plasmid pRV300 and contained two DNA fragments corresponding to the 3' end of lacG and the complete lacF gene. Four unique restriction sites were created, as well as a ribosome binding site that would allow the cloning and expression of new genes between these two fragments. Then, integration of the cloned genes into the lactose operon of L. casei could be achieved via homologous recombination in a process that involved two selection steps, which yielded highly stable food-grade mutants. This procedure has been successfully used for the expression of the E. coli gusA gene and the L. lactis ilvBN genes in L. casei. Following the same expression pattern as that for the lactose genes, beta-glucuronidase activity and diacetyl production were repressed by glucose and induced by lactose. This integrative vector represents a useful tool for strain improvement in L. casei that could be applied to engineering fermentation processes or used for expression of genes for clinical and veterinary uses.
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PMID:Integrative food-grade expression system based on the lactose regulon of Lactobacillus casei. 1105 30

When oil is spilled into aquatic systems, chemical dispersants frequently are applied to enhance emulsification and biological availability. In this study, a mammalian model system was used to determine the effect of Bonnie Light Nigerian crude oil, weathered for 2 d with continuous spraying and recirculation, and a widely used dispersant, Corexit (Cx) 9527, on intestinal microbial metabolism and associated populations. To determine the subchronic dose, concentrated or diluted (1:2, 1:5, 1:10, 1:20) Cx9527 or oil was administered by gavage to Fischer 344 rats and the effect on body weight was determined. Next, rats were treated for 5 wk with oil, dispersant, or dispersant + oil. Body and tissue weights, urine mutagenicity, and the impact on the intestinal microflora and three microbial intestinal enzymes linked to bioactivation were determined in the small and large intestines and cecum. Two tested dispersants, Cx9527 and Cx9500, were toxic in vitro (1:1,000 dilution), and oil was not mutagenic in strains TA98 and TA100(+/-S9). None of the treated rats produced urine mutagens detected by TA98 or TA100. Undiluted dispersant was lethal to rats, and weight changes were observed depending on the dilution, whereas oil generally was not toxic. In the 5-wk study, body and tissue weights were unaffected at the doses administered. Small-intestinal levels of azoreductase (AR), beta-glucuronidase (BG), and nitroreductase (NR) were considerably lower than cecal and large-intestinal activities at the same time point. A temporal increase in AR activity was observed in control animals in the 3 tissues examined, and large-intestinal BG activity was elevated in 3-wk controls. No significant changes in cecal BG activity were observed. Oil- or dispersant-treated rats had mixed results with reduced activity at 3 wk and elevated activity at 5 wk compared to controls. However, when the dispersant was combined with oil at 3 wk, a reduction in activity was observed that was similar to that of dispersant alone. One-week nitroreductase activity in the small intestine and cecum was unaffected in the three treatment groups, but elevated activity was observed in the large intestines of animals treated with oil or dispersant. The effect of the combination dose was not significantly different from the control value. Due to experimental error, no 3- or 5-wk NR data were available. By 5 wk of treatment, enterobacteria and enterococci were eliminated from ceca of oil-treated rats. When oil was administered in combination with dispersant, an apparent protective effect was observed on the enterococci and lactose-fermenting and nonfermenting enterobacteria. A more detailed analysis at the species level revealed qualitative differences dependent on the treatment. This study suggests that prolonged exposure of mammals to oil, dispersant, or in combination impacts intestinal metabolism, which ultimately could lead to altered detoxification of oil constituents and coexposed toxicants.
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PMID:Oral treatment of Fischer 344 rats with weathered crude oil and a dispersant influences intestinal metabolism and microbiota. 1143 62

With the aim of designing efficient expression systems for Lactobacillus casei, different factors affecting gene expression from the strong and highly modulated lac promoter have been systematically analyzed, by using the Escherichia coli beta-glucuronidase gene (gusA) as reporter. The activity of this enzyme (GUS) was quantified when plac:: gusA fusions were cloned in plasmids with different copy number or when gusA was inserted in the chromosomal lactose operon (single copy). Results showed a clear gene dosage effect and a positive influence of the native lac operon transcription and translation signals on GUS expression.
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PMID:Structural features of the lac promoter affecting gusA expression in Lactobacillus casei. 1217 41

Beta-glucuronidase is a lysosomal enzyme that plays an essential role in normal turnover of glycosaminoglycans and remodeling of the extracellular matrix components in both physiological and inflammatory states. The regulation mechanisms of enzyme activity and protein targeting of beta-glucuronidase have implications for the development of a variety of therapeutics. In this study, the effectiveness of various carbohydrate-immobilized adsorbents for the isolation of bovine liver beta-glucuronidase (BLG) from other glycosidases was tested. Beta-glucuronidase and contaminating glycosidases in commercial BLG preparations bound to and were coeluted from adsorbents immobilized with the substrate or an inhibitor of beta-glucuronidase, whereas beta-glucuronidase was found to bind exclusively with lactamyl-Sepharose among the adsorbents tested and to be effectively separated from other enzymes. Binding and elution studies demonstrated that the interaction of beta-glucuronidase with lactamyl-Sepharose is pH dependent and carbohydrate specific. BLG was purified to homogeneity by lactamyl affinity chromatography and subsequent anion-exchange high-performance liquid chromatography (HPLC). Lactose was found to activate beta-glucuronidase noncompetitively, indicating that the lactose-binding site is different from the substrate-binding site. Binding studies with biotinyl glycoproteins, lipids, and synthetic sugar probes revealed that beta-glucuronidase binds to N-acetyllactosamine/lactose-containing glycoconjugates at neutral pH. The results indicated the presence of N-acetyllactosamine/lactose-binding activity in BLG and provided an effective purification method utilizing the novel carbohydrate binding activity. The biological significance of the carbohydrate-specific interaction of beta-glucuronidase, which is different from the substrate recognition, is discussed.
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PMID:Novel carbohydrate-binding activity of bovine liver beta-glucuronidase toward lactose/N-acetyllactosamine sequences. 1677 8

Four ruminally fistulated multiparous Holstein cows were assigned to a 4x4 Latin square design with a 2x2 factorial arrangement of treatments to study the effects of dietary supplementation of monensin and flaxseed hulls on ruminal and milk concentration of the mammalian lignan enterolactone (EL) and ruminal and faecal activity of beta-glucuronidase. The hypothesis was that monensin supplementation has no effect on the incorporation of EL into milk when cows are fed flaxseed hulls. Treatments were: 1) control, neither flaxseed hulls nor monensin (CO); 2) diet containing (dry matter basis) 20% flaxseed hulls (FH); 3) diet with monensin (16 mg/kg of dry matter; MO); 4) diet containing 20% (dry matter basis) flaxseed hulls and 16 mg/kg monensin (HM). Intake of dry matter was higher for CO and MO than for FH and HM and monensin had no effect. Milk production decreased in cows fed flaxseed hulls while monensin had no effect. Production of 4% fat-corrected milk and concentrations of milk fat, lactose, urea N, and total solids were similar among treatments. Although there was a decrease in ruminal activity of beta-glucuronidase when feeding flaxseed hulls, the metabolism of plant into mammalian lignans may be increased as shown by enhanced concentration of EL in the rumen and milk. Supplementation with flaxseed hulls then may contribute to favourably change milk composition for better human health by enhancing mammalian lignan EL concentration.
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PMID:The interaction of monensin and flaxseed hulls on ruminal and milk concentration of the mammalian lignan enterolactone in late-lactating dairy cows. 1982 14

This study is reporting an outbreak of subclinical mastitis due to beta-hemolytic group L streptococci in an Austrian dairy herd with a history of high somatic cell count. At the first survey 16 of 33 lactating cows (28 quarters of 132) were cultured positive for beta-hemolytic, CAMP and esculin negative cocci that grew on Columbia blood agar with small grey catalase negative colonies. With the commercial API 20 Strep system (bioMerieux, F) isolates were classified as members of streptococci group L. All tested strains (eight of 28) produced acid from ribose, lactose, trehalose, amidon and glycogen; they hydrolysed hippurate and showed beta-glucuronidase, beta-galactosidase, alkaline phosphatase, leucinaminopeptidase and arginindehydrolase activity. Isolates were sensitive to bacitracin but resistant to tetracycline. Using phenotypic characterisation as well as sequence analysis of the 16S-23S intergenic spacer region of a representative strain, recovered isolates were identified as Streptococcus (S.) dysgalactiae ssp. equisimilis. Mastitis was characterized by normal milk secretions and absence of clinical abnormalities but high elevations of somatic cell count. Based on the characteristics of the strains and on the observations during the first herd survey, contagious transmission during milking as a result of poor milking hygiene was assumed. The mastitis was controlled through implementation of a strict hygiene protocol including use of single-use udder towels, post milking teat desinfection and cluster disinfection between milking cows in combination with antibiotic treatment of infected udders.
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PMID:[Outbreak of subclinical mastitis due to beta hemolytic group L streptococci (S. dysgalactiae ssp. equisimilis) in an Austrian dairy herd]. 2205 92


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