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Molecular cloning and transcriptional expression analysis of an intracellular beta-glucosidase, a family 3 glycosyl hydrolase, from the edible straw mushroom, Volvariella volvacea.

A beta-glucosidase, with a molecular mass of 95 kDa, was isolated from extracts of Volvariella volvacea mycelium grown on crystalline cellulose. Degenerate primers based on the N-terminal sequences of purified beta-glucosidase and two protease-generated peptides were used to generate cDNA fragments encoding a portion of the beta-glucosidase gene (bgl), and rapid amplification of cDNA ends was used to obtain full-length cDNA clones. The cDNA of bgl contained an ORF of 2586 bp coding for 862 amino acids. Alignment of the deduced amino-acid sequence of beta-glucosidase with deduced amino acid sequences of other microbial beta-glucosidases showed the highest overall homology with glycoside hydrolase family 3 beta-glucosidases from fungi. Transcripts of bgl were detected in total RNA extracted from mycelium grown on cellulose and cellobiose, and from mycelium pre-grown for 72 h in basal medium containing 1% (w/v) sorbitol following addition of alpha-lactose, beta-lactose, cellobiose, d- xylose, l-sorbose, beta-gentiobiose, sophorose or d-galactose. Addition of l-sorbose and d-glucosamine to mycelium grown on 1% (w/v) crystalline cellulose greatly increased the level of bgl expression. bgl Was expressed at various stages of the mushroom developmental cycle (substrate colonization to mature fruit body), although the number of bgl transcripts in pinhead and button stages was slightly smaller.

Agaricales↗

Microbial Production of Optically Pure l-Iditol by Yeast Strains.

Several yeast strains belonging to genus Candida were found to selectively hydrogenate l-sorbose with enantiomeric specificity, yielding optically pure l-iditol in the culture broth. The most active strain, isolated from a commercial lemon, was identified as Candida intermedia, which produced 50 g of l-iditol per liter from 150 g of l-sorbose per liter during a 5-day fermentation period (35% yield).

Journal Article↗

Isolation of Yersinia enterocolitica and related species from foods in France.

The occurrence of Yersinia enterocolitica and related species (Y. intermedia, Y. frederiksenii, Y. kristensenii) in foods from France was investigated by using different enrichment procedures. Initially, seven procedures were evaluated with pork products. These methods included a cold preenrichment in yeast extract-rose bengal broth or in phosphate-sorbitol-bile medium, followed by selective enrichment either in Pastone-sucrose-Tris-azide broth, in modified Rappaport broth, or in bile-oxalate-sorbose broth, and then isolation onto Hektoen or cefsulodin-irgasan-novobiocin agar with or without KOH pretreatment. The best enrichment procedure in terms of percentage of positive samples obtained within the shortest time was the combination of phosphate-sorbitol-bile and bile-oxalate-sorbose with alkali treatment before isolation onto cefsulodin-irgasan-novobiocin agar. This system was then used to analyze foods other than pork. An average contamination rate of 33.5% was observed for 666 samples analyzed; pork products were by far the most contaminated, especially the so-called tartinette (96.8% of positive samples) which contained up to five different strains of Yersinia spp. Environmental serogroups of Y. enterocolitica O:5, O:39,41, O:6, and O:7,8 were predominant, but no isolate of either human pathogenic type (O:3 or O:9) was obtained.

Animals↗

EFFECT OF SUGARS AND OTHER CARBON COMPOUNDS ON GERMINATION AND POSTGERMINATIVE DEVELOPMENT OF BACILLUS MEGATERIUM SPORES.

Hyatt, Mildred T. (Pioneering Research Division. U.S. Army Natick Laboratories, Natick, Mass.), and Hillel S. Levinson. Effect of sugars and other carbon compounds on germination and postgerminative development of Bacillus megaterium spores. J. Bacteriol. 88:1403-1415. 1964.-A total of 77 carbon-containing compounds were tested for their ability to support germination and postgerminative development of Bacillus megaterium spores. The only effective germination agents were certain of the hexose sugars and their derivatives. With unheated spores, only d-glucose, d-mannose, 2-deoxy-d-glucose, d-glucosamine, and N-acetyl-d-glucosamine (all at 25 mm) supported appreciable germination (ca. 25%). Heat-shock at 60 C for 10 min increased germination and decreased the concentration of sugar required for germination, so that these compounds, at 2.5 mm, supported 40 to 60% germination. Higher concentrations (25 mm) of other compounds, d-fructose, l-sorbose, d-allose, d-altrose, 2-hydroxyethyl-d-glucose, and beta-methyl-d-glucoside, were required for appreciable germination of heated spores. Glucose or mannose contamination accounted for the germination apparently induced by certain other sugars. Ionic contamination did not appear to contribute to the germination induced by d-glucose, d-fructose, 2-deoxy-d-glucose, or l-sorbose. There was no clear-cut evidence for a multiplicity of metabolic pathways in the triggering of B. megaterium spore germination by various sugars. Postgerminative development of germinated spores was supported by a wider variety of carbon compounds, including some pentoses and hexoses, many oligosaccharides, sugar derivatives, some alcohols, and some of the tricarboxylic acid cycle intermediates. Compounds effective for germination were not necessarily utilizable for growth, and vice versa. Oxygen consumption rates reflected the progress and extent of postgerminative development on the various carbon compounds. Utilization of glucose during postgerminative development was followed, and the concentration requirements were determined.

Acetylglucosamine↗

Glucose-induced Release of Amino Acids from Saccharomyces carlsbergensis by Action on the Cytoplasmic Membrane.

When washed yeast cells grown under appropriate conditions were suspended in glucose solution there was a sudden release of alpha-amino nitrogen into the medium. This released material was of low molecular weight, and its composition was closely similar to that of the intracellular free amino acid pool. During the leakage of amino acids, the yeast did not efficiently absorb labeled amino acids added to the test medium, despite the rapid uptake and metabolism of glucose. Uptake of a labeled amino acid and reabsorption of the released alpha-amino nitrogen occurred almost simultaneously. When these yeast cells were exposed to glucose in the presence of calcium ions, leakage was strongly inhibited. Butanol under the same conditions increased glucose-induced leakage of cell contents. The adenosine triphosphatase activity of intact yeast cells exposed to glucose was greater than that of cells exposed to water. Yeast cells treated with glucose prior to equilibration with sorbose exhibited less ability to retain the sorbose when washed at 0 C than did cells pretreated with water. It was concluded that glucose-induced leakage of amino acids was the result of two factors acting together. These were (i) a change in membrane permeability associated with glucose uptake, and (ii) a temporary shortage of energy for amino acid uptake or retention.

Journal Article↗

Characterisation of Yersinia species isolated from a kennel and from cattle and pig farms.

Between April 1984 and November 1986, 126 faeces samples were collected from puppies and bitches in a kennel and examined for Yersinia species; 45 (35.7 per cent) of them were positive. Thirty-eight isolates were Y enterocolitica, five were Y frederiksenii and two were Y intermedia. Twenty-one of the Y enterocolitica isolates belonged to serogroup 0:3 and 17 of these were L-sorbose negative; all these isolates were from puppies. One strain of Y frederiksenii and all the L-sorbose-negative Y enterocolitica serogroup 0:3 isolates were resistant to antimicrobial agents and showed four different patterns of resistance (ampicillin, cephalothin and tetracycline; ampicillin, cephalothin, streptomycin and tetracycline; ampicillin, chloramphenicol, cephalothin, streptomycin and sulfathiazole; and ampicillin, chloramphenicol, cephalothin, streptomycin, sulfathiazole and tetracycline. In January 1986, investigations were conducted on a cattle farm and a pig farm close to the kennel. Of 19 bovine faeces samples 11 (57.8 per cent) were positive for Yersinia species; eight yielded Y enterocolitica and four yielded Y frederiksenii. None of the Y enterocolitica isolates belonged to serogroup 0:3. Of 20 porcine faeces samples eight (40 per cent) were positive for Yersinia species; all eight yielded Y enterocolitica and four also yielded Y pseudotuberculosis. Two of the isolates of Y frederiksenii and two of the isolates of Y enterocolitica from the farms had the following resistance patterns: ampicillin, cephalothin and streptomycin; ampicillin, streptomycin and tetracycline; ampicillin, chloramphenicol, cephalothin, streptomycin, trimethoprim-sulphamethoxazole and tetracycline; and ampicillin, chloramphenicol, cephalothin, streptomycin, sulphatiazole, trimethoprim-sulphamethoxazole and tetracycline.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Purification and molecular characterization of a quinoprotein alcohol dehydrogenase from Pseudogluconobacter saccharoketogenes IFO 14464.

We have cloned and verified a gene for a novel quinoprotein alcohol dehydrogenase (ADH) from Pseudogluconobacter saccharoketogenes IFO 14464 that has the ability to oxidize L-sorbose to 2-keto-L-gulonic acid (2-KLGA). The enzyme was purified from the soluble fraction of the bacterium and was estimated to be a monomeric protein with a molecular weight of 65 kDa from the analyses of SDS-PAGE and gel-filtration chromatography. An open reading frame of 1824 bp for 608 amino acid residues was estimated as the gene for ADH because of the consistency of the calculated molecular mass and the elucidated partial amino acid sequences of the native enzyme. Homology search revealed that the enzyme showed close similarity to quinoprotein alcohol dehydrogenases isolated from Methylobacterium extorquens and Acetobacter aceti, particularly in the tryptophan docking motifs in the alpha-subunits of those dehydrogenases. The ability to convert L-sorbose to 2-KLGA was found when the lysate of recombinant Escherichia coli DH10B transformed with the gene for ADH was mixed with CaCl2and pyrroloquinoline quinone (PQQ). These data indicate that the cloned DNA is the desired gene for the ADH in which CaCl2 and PQQ are essential for enzymatic activity.

Journal Article↗

Feeding responses by adult males of Melanoplus sanguinipes (Fabricius) to carbohydrates and amino acids.

Adult males of Melanoplus sanguinipes (Fabricius), the migratory grasshopper, were starved for 18 h and were placed, one per arena, into arenas containing treated glass-fibre discs. The discs had been dipped into aqueous solutions of carbohydrates or amino acids of 0.0001, 0.001, 0.01, or 0.1 M concentration and allowed to dry at air temperature. They were placed vertically on pins and distributed at random among five equidistant stations around the periphery of the bottom of the arena. Each arena was provided with a glass-fibre disc that had been dipped in distilled water, as a control. The grasshoppers were allowed to feed at room temperature at 16:8 (L:D) for 24 h. Determinations of the effects of nutrient chemicals on feeding were determined by dry-weight differences between the weights of the treated discs before and after testing. Ribose, glucose, mannose and trehalose had no influence on feeding; 0.01 M fructose of 0.1 M arabinose, galactose, melibiose or sucrose increased feeding over that obtained with the control discs (P = 0.05); and 0.01 M xylose or sorbose depressed feeding. Each of the 11 amino acids investigated was phagodeterrent to adult males of M. sanguinipes. The present results confirm the variability of responses to carbohydrates among acridids; however, the reversal of phagodeterrency of sorbose or xylose at 0.1 M concentration is believed to be the first reported instance of such behaviour. In contrast to other reports of phagostimulation of acridids by individual amino acids or amino-acid mixtures, all protein amino acids tested in the present study were phagodeterrent to adult males of M. sanguinipes, even at low concentrations.

Amino Acids↗

[Unusual coordination behavior of D-fructose towards dimethyltin(IV)2+: metal-promoted deprotonation of alcoholic hydroxyl groups in aqueous solutions at low pH].

To study the effect of the conformation of sugar hydroxy groups on metal complexation processes, complex formation of eight saccharides (D-fructose, L-sorbose, L-arabinose, D-arabinose, D-glucose, D-sorbitol, 2-deoxy-D-glucose and D-saccharose) with dimethyltin(IV)2+ cations was investigated in aqueous solution by potentiometric equilibrium measurements, 13C NMR, polarimetric and Mössbauer spectroscopic methods. The experimental results proved that deprotonation of D-fructose and L-sorbose is caused by the coordination of dimethyltin(IV)2+ in the unusual low pH interval 4-6 in contrast to the other saccharides deprotonated in analogous way at pH > 8. Increasing the pH of the solution resulted in the formation of further complexes. Stability and composition of the species was determined by potentiometric studies. 13C NMR measurements led to the assignment of the sugar OH groups participating in the processes. Mössbauer investigations in the quick-frozen solutions permitted the determination of the stereochemistry of tin(IV) in the complexes.

Alcohols↗

[Effect of growth medium composition of glucoamylase and glycosyltransferase activity of Endomyces fibuliger].

Production of glucoamylase and glycosyltransferase by Endomyces fibuliger was found to depend on sources of carbon and nitrogen nutrition. Starch at a concentration above 0.5% in the medium stimulated biosynthesis of glycosyltransferase but inhibited production of glucoamylase by End. fibuliger 20-9. The rate of growth of the micro-organism increased by a factor of 3.3 with an increase of starch concentration from 0.5 to 6%. Synthesis of glycosyltransferase was repressed by glucose, lactose, sucrose and maltose. Synthesis of glucoamylase was repressed by lactose, sorbose and galactose. Synthesis of glycosyltransferase was stimulated by xylose, sorbose and galactose. Production of glucoamylase was stimulated by xylose and arabinose. Growth of the culture and synthesis of glucoamylase and maltase in the cultural broth were stimulated by an increase in the concentration of maize extract. Biosynthesis of glucoamylase and glycosyltransferase was stimulated by NH4H2PO4.

Ascomycota↗

UV and X-ray sensitivity of Candida albicans laboratory strains and mutants having chromosomal alterations.

Utilization of L-sorbose, D-arabinose or primary fluconazole resistance in Candida albicans are controlled by copy number of specific chromosomes. On the other hand, spontaneous morphological mutants have a wide range of chromosomal alterations. We have investigated the UV and X-ray sensitivity of these mutants, as well as C. albicans laboratory strains. While L-sorbose utilizing mutants had normal sensitivities, a large subclass of D-arabinose utilizing mutants was abnormally sensitive to UV. Spontaneous morphological mutants responded differently, an expected result because of the heterogeneous nature of their electrophoretic karyotypes. We suggest that the differences in UV and X-ray sensitivity are due to gene imbalance caused by some chromosomal alterations. In this respect, the radiation sensitivity is similar to other features impaired by changes in chromosomes, but is unlike the acquisition of the ability to utilize alternative nutrients or the acquisition of resistance to fluconazole. Our studies also revealed that strains of C. albicans heterozygous for the mating type loci exhibited the same X-ray sensitivity as homozygous or hemizygous strains, a finding which is in contrast to the properties of Saccharomyces cerevisiae, where heterozygous strains are more resistant. This feature of C. albicans strains may be indicative of an inefficient repair system that may be related to inefficiency of mating.

Journal Article↗

[Integration and expression of sdh gene in Escherichia coli].

The chloramphenicol-resistant cassette with short shared sequences of ptsG gene on both ends was PCR-generated from plasmid pKF3 and ligated to pMD18-T to construct pMD18-PC. The sdh gene for sorbose dehydrogenase was generated from plasmid pQE60-SDH and inserted into pMD18-PC, then pMD18-PC-SDH was constructed. It was digested with Pvu II and the target fragment ptsG1-cat-sdh-ptsG2 was recovered and electroporated into Escherichia coli JM109/pKD46. Homologous-recombination between linear DNA cassettes and Escherichia coli chromosomes took place by Red recombination. The detection result showed that the integron JM109s was of sorbose dehydrogenase activity. The PCR products assay using the upstream and downstream sequences of ptsG gene as primers and JM109s genomic DNA as template, indicated that sdh gene had been integrated at the ptsG gene site in Escherichia coli.

Anti-Bacterial Agents↗

Metabolic engineering study on the direct fermentation of 2-keto-L-gulonic acid, a key intermediate of L-ascorbic acid in Pseudomonas putida IFO3738.

We have achieved production of 2-keto-L-gulonic acid (2-KLGA) in recombinant Pseudomonas putida IFO3738. Firstly, the genes for sorbose dehydrogenase (SDH)/sorbosone dehydrogenase (SNDH) were introduced into P. putida. The recombinant P. putida/pBBR-SDH produced 0.7 mg/ml of 2-KLGA in a culture broth containing 5% L-sorbose. Replacement of the native SNDH promoter by the Escherichia coli tufB promoter (pBBR-SDH-tufB) improved the productivity of 2-KLGA up to 11.4 mg/ml. Secondly, the sorbitol dehydrogenase (SLDH) gene was also introduced into P. putida. The recombinant P. putida/pUCP19-3DH carrying the genes for SDH, SNDH and SLDH had the ability to produce 2-KLGA (7.5 mg/ml) in a 5% d-sorbitol broth. The productivity of 2-KLGA was improved up to 9.8 mg/ml by changing to an expression system with two plasmids, pBBR-SDH-tufB (for SDH/SNDH) and pUCP19-SLDH (for SLDH), respectively. Moreover, the replacement of the native SLDH promoter by the E. coli tufB promoter (pUCP19-SLDH-tufB) improved the 2-KLGA productivity up to 11.6 mg/ml. Optimization of cultivation conditions increased the conversion yield of 2-KLGA to 32% and that of l-idonate, a metabolite of 2-KLGA, to 40%. These results indicate P. putida IFO3738 is one of the candidate strains for direct fermentation of 2-KLGA.

Journal Article↗

[The thiobarbituric method for analyzing sugars. III. A method for studying sorbitol dehydrogenase activity].

A method for studying of sorbitol dehydrogenase activity of Acetobacter suboxydans has been worked out which can be applied to other microbe cells too. The enzyme transformation of D-sorbitol into L-sorbose is determined through the reaction between ketohexose and 2-thiobarbituric acid under heating in 1 M oxalic acid (pH = 0.64) medium for 15 or 30 min. The yellow-coloured product was measured at 400 nm. The method is characterized with its high specificity, good reproducibility and accuracy, which allows for its application for quantitative analysis of sorbitol in dietetic foods. For this purpose a sorbitol dehydrogenase preparation isolated from bacterial cells is needed. The main purpose of the spectrophotometric method is to use it as a control in the process of microbial transformation of sorbitol into sorbose both under laboratory and industrial conditions.

Acetobacter↗

[Influence of culture media on the growth of Streptococcus mutans ATCC 25175 in the presence of various carbohydrates and their derivatives].

The growth of Streptococcus mutans ATCC 25 175 has been studied in the presence of various sugars (sorbitol, mannitol, lycasin, sorbose and xylitol) and compared to sucrose, glucose and fructose, added to a complex and a synthetic culture medium. In these two media, the decrease in pH was related to the bacterial growth; this fact was confirmed by the dosages of the liberated lactic acid. In the complex medium, the different sugars influenced only slightly the bacterial growth, whereas in the synthetic medium the micro-organisms did not grow in the presence of sorbose, xylitol or lycasin 80/55. An adaptation period was necessary before the beginning of bacterial growth in the synthetic medium supplemented with sorbitol and mannitol.

Carbohydrates↗

The sugar phosphate specificity of rat hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

The sugar phosphate specificity of the active site of 6-phosphofructo-2-kinase and of the inhibitory site of fructose-2,6-bisphosphatase was investigated. The Michaelis constants and relative Vmax values of the sugar phosphates for the 6-phosphofructo-2-kinase were: D-fructose 6-phosphate, Km = 0.035 mM, Vmax = 1; L-sorbose 6-phosphate, Km = 0.175 mM, Vmax = 1.1; D-tagatose 6-phosphate, Km = 15 mM, Vmax = 0.15; and D-psicose 6-phosphate, Km = 7.4 mM, Vmax = 0.42. The enzyme did not catalyze the phosphorylation of 1-O-methyl-D-fructose 6-phosphate, alpha- and beta-methyl-D-fructofuranoside 6-phosphate, 2,5-anhydro-D-mannitol 6-phosphate, D-ribose 5-phosphate, or D-arabinose 5-phosphate. These results indicate that the hydroxyl group at C-3 of the tetrahydrofuran ring must be cis to the beta-anomeric hydroxyl group and that the hydroxyl group at C-4 must be trans. The presence of a hydroxymethyl group at C-2 is required; however, the orientation of the phosphonoxymethyl group at C-5 has little effect on activity. Of all the sugar monophosphates tested, only 2,5-anhydro-D-mannitol 6-phosphate was an effective inhibitor of the kinase with a Ki = 95 microM. The sugar phosphate specificity for the inhibition of the fructose-2,6-bisphosphatase was similar to the substrate specificity for the kinase. The apparent I0.5 values for inhibition were: D-fructose 6-phosphate, 0.01 mM; L-sorbose 6-phosphate, 0.05 mM; D-psicose 6-phosphate, 1 mM; D-tagatose 6-phosphate, greater than 2 mM; 2,5-anhydro-D-mannitol 6-phosphate, 0.5 mM. 1-O-Methyl-D-fructose 6-phosphate, alpha- and beta-methyl-D-fructofuranoside 6-phosphate, and D-arabinose 5-phosphate did not inhibit. Treatment of the enzyme with iodoacetamide decreased sugar phosphate affinity in the kinase reaction but had no effect on the sensitivity of fructose-2,6-bisphosphatase to sugar phosphate inhibition. The results suggest a high degree of homology between two separate sugar phosphate binding sites for the bifunctional enzyme.

Animals↗

Some physiological studies on Penicillium expansum Link.

Penicillium expansum Link showed excellent/good growth on all carbohydrates except ribose, lactose, sorbose and sucrose, which induced fair or poor growth. It made excellent growth on mannitol and dulcitol while the rest of the carbon sources were either poorly utilized or not utilized. Sorbose neither inhibited nor promoted growth of the pathogen in the presence of good carbon sources. The pathogen showed fair/poor growth on cystine, phenylalanine, histidine, mono-HCl, histidine di-HCl, ammonium sulphate, ammonium nitrate, ammonium chloride, ammonium phosphate, and urea, while the rest of the nitrogen sources induced excellent/good growth. However, there was no growth on potassium nitrite. Cystine inhibited the growth of the pathogen to some extent in the presence of good amino acids, i.e. serine proline, methionine, arginine mono-HCl, tyrosine and tryptophane, and not at all were inhibited in the presence of the remaining amino acids.

Alcohols↗

Photoregulation of cot-1, a Kinase-Encoding Gene Involved in Hyphal Growth in Neurospora crassa.

Blue light plays a key role as an environmental signal in the regulation of growth and development of fungi and plants. Here we demonstrate that in Neurospora crassa hyphae branch more frequently in cultures grown in light. Previous studies had identified cot-1 as a gene that controls apical hyphal cell elongation. In the cot-1 mutant, cessation of elongation is accompanied by hyperbranching. Here we demonstrate that the cot-1 gene encodes two transcript species of about 2100 nt (cot-1 (s)) and about 2400 nt (cot-1 (l)) in length and that the ratio of both transcript species abundance is photoregulated. The origin of the difference between cot-1 (l) and cot-1 (s) was localized to the 5' end of the cot-1 transcripts, suggesting that two COT1 isoforms with different activities may be formed. Both light effects, on branching and on cot-1 expression, were dependent on functional wc-1 and wc-2 gene products. In addition to light, l-sorbose comprises another environmental cue that controls hyphal branching in N. crassa. In the presence of l-sorbose, photoregulation of cot-1 was blocked, suggesting the involvement of alternative and potentially interdependent signaling pathways for the regulation of hyphal elongation/branching. Copyright 1998 Academic Press.

Journal Article↗