Extracellular β-d-fructofuranosidase elaborated by streptococcus salivarius strain 51: preparation, and mode of action on a levan and on homologues of inulobiose

Marshall, Keith; Weigel, Helmut

doi:10.1016/s0008-6215(00)84543-7

Cited by 11 publications

(3 citation statements)

References 10 publications

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“…The data obtained by "C-NMR with fractions of S. salivarius levan are in accord with this view ). The spherical shape may thus allow the levan to be retained in dental plaque by virtue of its low diffusive properties, while being effectively hydrolysed from its outermost regions by exo-hydrolyases (Da Costa & Gibbons, 1968;Fhrlich et al, 1975;Marshall & Weigel, 19806). Enzymatic degradation of the levan produced by S. salivarius followed by linkage analysis supports this view.…”

Section: Streptococcimentioning

confidence: 98%

The fructosyltransferase of Streptococcus salivarius

Jacques

1993

New Phytologist

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Section: Streptococcimentioning

confidence: 98%

The fructosyltransferase of Streptococcus salivarius

Jacques

1993

New Phytologist

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“…The induction of fructanase in oral streptococci grown in the presence of D-fructan has been demonstrated in several studies (Dacosta & Gibbons, 1968;van Houte & Jansen, 1968;Marshall & Weigel, 1980). More recently, strains of Streptococcus mutans serotypes a, d and d/g were shown to release fructanase when grown in batch culture in the absence of fructan in a complex medium supplemented with glucose (Walker et al, 1983).…”

Section: Introductionmentioning

confidence: 93%

Inducible and Constitutive Formation of Fructanase in Batch and Continuous Cultures of Streptococcus mutans

1985

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The production of extracellular beta-D-fructanase by several strains of Streptococcus mutans was studied in continuous culture. When glucose was the limiting nutrient, S. mutans K1-R and OMZ176 accumulated fructanase to maximum levels at low growth rates (dilution rate 0.05-0.10 h-1), due to the longer residence times of the bacteria in the culture vessel under these conditions. Extracellular fructanase activity was greater than has been previously reported for batch cultures. The rate of fructanase production for both S. mutans strains K1-R and OMZ176 increased with increasing growth rate when glucose was limiting. Under conditions of glucose sufficiency, the rate of fructanase production was always lower than in cultures where glucose was limiting, irrespective of the growth rate. Cultures of S. mutans Ingbritt (serotype c) grown with sorbitol- or glucose-limitation synthesized fructanase at a very low basal rate. When fructose was the limiting carbohydrate the enzyme was induced with a maximum rate of production occurring at a dilution rate of 0.40 h-1. Strains of S. mutans from other serotypes (a, d, d/g) were either not affected by changing the limiting sugar from glucose to fructose or else fructanase activity was slightly decreased in the fructose-limited medium. Fructanases from various strains of S. mutans readily hydrolysed (2----6)-beta-D-fructans, but all possessed the ability to hydrolyse (2----1)-beta-D-fructans to varying degrees.

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“…Invertase has been purified and characterized from many higher plant sources like sugarcane [2] or chickpea (Cicerariefinum) [3]. This enzyme has also been found isolated from a large number of other organisms such as fungi (Aspergillus ficuum [4], Aspergillus nidulans [5], Pycnoporus sanguineus [6] and Aspergillus niger [7]), yeasts (Saccharomyces cerevisiae [8,9], Schwanniomyces occidentalis [10], Schizosaccharomyces pombe [11], Kluyveromyces fragilis [12], Pichia anomala [13] and Presented at Balaton Symposium on High Performance Separation Methods, Si6fok, Hungary, September [1][2][3]1999 Candida utilis [14,15]) and bacteria (Streptococcus salivarius [16] and Zymomonas mobilis [ 17]). The fungi are a good source of invertase, especially because, in some cases, this enzyme, after synthesis, is secreted into the liquid medium.…”

Section: Introductionmentioning

confidence: 99%

The optimization of the liquid affinity chromatography conditions of the extracellular invertase isolation from theCandida utilis cultures

et al. 2000

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SummaryThe Candida utilis yeast strain was used as a source for the extracellular invertase (E.C.3.2.1.26). The conditions for the highest extracellular invertase activity production were established using three liquid media. The enzyme was purified using one-step affinity chromatography method in the optimized conditions. Three saccharides: sucrose, maltose and inulin were comparatively used as ligands in the affinity technique. The partially purified invertase was afterwards immobilized on the newly described solid matrix with keratin as an activator.

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Extracellular β-d-fructofuranosidase elaborated by streptococcus salivarius strain 51: preparation, and mode of action on a levan and on homologues of inulobiose

Cited by 11 publications

References 10 publications

The fructosyltransferase of Streptococcus salivarius

The fructosyltransferase of Streptococcus salivarius

Inducible and Constitutive Formation of Fructanase in Batch and Continuous Cultures of Streptococcus mutans

The optimization of the liquid affinity chromatography conditions of the extracellular invertase isolation from theCandida utilis cultures

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