Studies on dextrans and dextranases. 3. Structures of oligosaccharides from <i>Leuconostoc mesenteroides</i> (Birmingham) dextran

Bourne, E. J.; Hutson, D. H.; Weigel, Helmut

doi:10.1042/bj0860555

Cited by 40 publications

(11 citation statements)

References 16 publications

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“…2). Most fungal dextranases that have been investigated are extracellular (5,6,10), although an intracellular fungal dextranase has been studied (30). Bifidobacterium bifidus produces an extracellular dextranase (1)(2)(3)12), and a soil bacterium has been isolated which produces at least two extracellular dextranases and some intracellular dextranase activity (11,39).…”

Section: Discussionmentioning

confidence: 99%

Detection and Preliminary Studies on Dextranase-Producing Microorganisms from Human Dental Plaque

1973

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An enriched nutrient agar medium containing blue dextran has been utilized for the detection of dextranase-producing microorganisms in human dental plaque. When compared with the total viable anaerobic plaque flora, the proportion of these microbes in supragingival plaque from different individuals varied over a wide range. Preliminary characterization of some of the dextranaseproducing microorganisms revealed a heterogeneous mixture of cell types with varying morphological and biochemical characteristics. Several bacterial isolates were tentatively identified as being members of the genus Actinomyces. An additional isolate appeared to belong to the genus Bacteroides. The dextrandegrading enzymes produced by these bacteria are extracellular, and a cell-free preparation from one of the isolates has been shown to cause extensive endohydrolytic cleavage of high-molecular-weight dextrans.

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Section: Discussionmentioning

confidence: 99%

Detection and Preliminary Studies on Dextranase-Producing Microorganisms from Human Dental Plaque

1973

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“…The separate purified oligosaccharides were subjected to enzymatic degradation using dextranase from Penicillium sp. (EC 3.2.1.11; Sigma, St. Louis, MO), which hydrolyzes only ␣-(136)glucosidic bonds (3,26), amyloglucosidase from Aspergillus niger (EC 3.2.1.3; Sigma), which was shown to hydrolyze ␣-(134), ␣-(133), and ␣-(136) linkages at decreasing rates, respectively, to produce glucose from the nonreducing end of linear oligosaccharides (21,22) and ␣-glucosidase from Bacillus stearothermophilus (EC 3.1.2.20; Megazyme, Ireland), which hydrolyzes terminal, ␣-(134) linkages from the nonreducing end of oligosaccharides to produce glucose (17). Oligosaccharides (1 g · l Ϫ1 ) were incubated with 0.1 U ml Ϫ1 amyloglucosidase, 66 U ml Ϫ1 dextranase, and 66 U ml Ϫ1 ␣-glucosidase.…”

Section: Vol 71 2005 Highly Hydrolytic Reuteransucrase From L Reutmentioning

confidence: 99%

Highly Hydrolytic Reuteransucrase from Probiotic Lactobacillus reuteri Strain ATCC 55730

Kralj

Stripling

Sanders

et al. 2005

Appl Environ Microbiol

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Lactobacillus reuteri strain ATCC 55730 (LB BIO) was isolated as a pure culture from a Reuteri tablet purchased from the BioGaia company. This probiotic strain produces a soluble glucan (reuteran), in which the majority of the linkages are of the ␣-(134) glucosidic type (ϳ70%). This reuteran also contains ␣-(136)-linked glucosyl units and 4,6-disubstituted ␣-glucosyl units at the branching points. The LB BIO glucansucrase gene (gtfO) was cloned and expressed in Escherichia coli, and the GTFO enzyme was purified. The recombinant GTFO enzyme and the LB BIO culture supernatants synthesized identical glucan polymers with respect to linkage type and size distribution. GTFO thus is a reuteransucrase, responsible for synthesis of this reuteran polymer in LB BIO. The preference of GTFO for synthesizing ␣-(134) linkages is also evident from the oligosaccharides produced from sucrose with different acceptor substrates, e.g., isopanose from isomaltose. GTFO has a relatively high hydrolysis/transferase activity ratio. Complete conversion of 100 mM sucrose by GTFO nevertheless yielded large amounts of reuteran, although more than 50% of sucrose was converted into glucose. This is only the second example of the isolation and characterization of a reuteransucrase and its reuteran product, both found in different L. reuteri strains. GTFO synthesizes a reuteran with the highest amount of ␣-(134) linkages reported to date.

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“…Dextrans. The dextrans used in the present study have been described previously (23)(24)(25)(26)(27)(28)(29)(30). The proportions of a(1---~6), a(1--*3)-like, and a(1--*4)-like linkages in the dextrans used are summarized in Table I according to the previous reports (24)(25)(26).…”

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confidence: 99%

“…Glucose, methyl a-D-glucoside, methyl-/~-D-glucoside, trehalose, cellobiose, gentiobiose, kojibose, panose, isomaltose (IM2), isomaltotriose (IM3), isomaltopentaose (IM5), isomaltohexaose (IM6), isomaltoheptaose (IM7), nigerose (N2), nigerotriose (N3), nigerotetraose (N4), nigeropentaose (N5), nigerohexa-heptaose (N6, 7), maltose (M2), maltotriose (M3), maltotetraose (M4), maitopentaose (M5), maltohexaose (M6), and maltoheptaose (M7), and branched oligosaccharides whose structures are shown in Fig. 1 have been described previously (10,11,17,27,28). Isopanosyla(1--*4)isopanose isolated from pullulan was kindly provided by Dr. T. Sawai, Aichi Kyoiku University and three trisaccharides: DGlca(1---~6)-DGlca Immunochemicul Assay.…”

mentioning

confidence: 99%

Immunochemical specificity of the combining site of murine myeloma protein CAL20 TEPC1035 reactive with dextrans.

Sugii¹,

Kabat²,

Shapiro³

et al. 1981

The Journal of Experimental Medicine

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The immunochemical specificity of the combining sites of murine myeloma protein CAL20 TEPC1035 was studied by quantitative precipitin and precipitin inhibition assays. Myeloma protein CAL20 TEPC1035 precipitated with only three dextrans, B1355S4, B1498S, and B1501S, with high proportions of alpha(1 leads to 3) linkages, but not with any other dextrans, glycogen, and pullulan. Inhibition tests with various sugars show that the combining site of myeloma protein CAL20 TEPC1035 is most complementary to panose, a trisaccharide DGlc alpha(1 leads to 6)DGlc alpha(1 leads to 4)DGlc. Panose was 3.3 times more potent than a tetrasaccharide DGlc alpha(1 leads to 6)DGlc alpha(1 leads to 4)DGlc alpha(1 leads to 4)DGlc and 8, 23, 42, > 42 times more active than maltose, nigerose, isomaltose, and kojibiose, respectively. These findings were paralleled by their binding properties as determined by affinity electrophoresis. The association constants (Ka) of these three dextrans to myeloma protein CAL20 TEPC1035 ranged from 3.8 X 10(3) ml/g to 5.02 X 10(3) ml/g. The association constant of inhibitor (Kia) of panose was 8.19 X 10(3) M-1. Myeloma protein CAL20 TEPC1035 is an antidextran with specificity different from those of other murine myeloma antidextrans and from human antidextrans reported previously and its combining site size is at least as large as a trisaccharide. The binding constant of methyl alpha-D-glucoside (7.2 X 10(2)) was 73% of that of panose and comparable to that of myeloma protein W3129 (9.4 X 10(2)) with a cavity-type site and 600 times lower (1.6 X 10(0)) for QUPC52 with a groove type site, indicating that the terminal nonreducing residue is held in a cavity. Inhibition data with various alpha(1 leads to 4)-linked oligosaccharides also indicate that the internal portions of these inhibitors may react directly with a portion of the combining site. These findings suggest that myeloma antidextran CAL20 TEPC1035 has a partial cavity-type combining site in which the terminal nonreducing dGlc alpha(1 leads to 6) moiety is held in a cavity with the other two sugars forming a groove. However, oligosaccharides with one or more alternating [leads to 3DGlc alpha(1 leads to 6)DGlc alpha(1 leads to 3)DGlcl leads to] units with and without terminal nonreducing DGlc alpha(1 leads to 6) or DGLc alpha(1 leads to 3) side chains remain to be tested to determine whether structures known to be present in the three dextrans which precipitate CAL20 TEPC1035 may not prove to be more active than panose.

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Studies on dextrans and dextranases. 3. Structures of oligosaccharides from Leuconostoc mesenteroides (Birmingham) dextran

Cited by 40 publications

References 16 publications

Detection and Preliminary Studies on Dextranase-Producing Microorganisms from Human Dental Plaque

Detection and Preliminary Studies on Dextranase-Producing Microorganisms from Human Dental Plaque

Highly Hydrolytic Reuteransucrase from Probiotic Lactobacillus reuteri Strain ATCC 55730

Immunochemical specificity of the combining site of murine myeloma protein CAL20 TEPC1035 reactive with dextrans.

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