Purification and characteristics of two exoinulinases from Chrysosporium pannorum

Xiao, Rong; Tanida, Masatoshi; Sugiyama, Takao

doi:10.1016/0922-338x(89)90250-x

Cited by 29 publications

(18 citation statements)

References 13 publications

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“…However, the purified hydrolase described here and the highly purified hydrolase from Dactilys glomerata reported by Yamamoto and Mino (1985) hydrolyze both P-2,6-and P-2,l-fructans but do not hydrolyze SUC. Simpson and Bonnett (1993) O that hydrolyzes SUC, P-2,1-and P-2,6-linked fructans in the microbial literature (Xaio et al, 1989;Blatch and Woods, 1993). To our knowledge no enzymes have yet been purified from a higher plant that can hydrolyze a11 three linkages.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of an Oat Fructan Exohydrolase That Preferentially Hydrolyzes [beta]-2,6-Fructans

Henson

Livingston

1996

Plant Physiol.

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Oat (Avena sativa cv Fulghum) fructan hydrolase was purified by ammonium sulfate precipitation and anion-exchange, hydrophobic interaction, and size-exclusion chromatography. The enzyme was purified to homogeneity as determined by the presence of a single band (43 kD) on a silver-stained sodium dodecyl sulfate-polyacrylamide gel. A mixture of /3-2,6-linked fructan (neokestin) isolated from oat was used as the substrate to purify fructan hydrolase. Neokestin and small degree of polymerization fructan isomers were used to characterize the substrate specificity of the purified enzyme. The purified fructan hydrolase catalyzed hydrolysis of the terminal p-2,6 linkage of 6G,6-kestotetraose 3.5 times more rapidly than it hydrolyzed the terminal p-2,6 linkage of 6G-kestotriose and approximately 1 O times faster than it hydrolyzed the terminal p-2,1 linkage of chicory inulin. Sucrose and I-kestose were not substrates. The K, for neokestin (p-2,6-linked fructans with a degree of polymerization of 7-14) hydrolysis was 2.8% (w/v), and the V,,, was 0.041 pmol min-' mL-'. The K,,, for hydrolysis of 6C,6-kestotetraose was 5.6% (w/v), and the V,,, was 0.1 38 pmol min-' mL-'. Catalysis was exolytic and by multiple chain attack. Hydrolysis of neokestin was maximal at pH 4.5 to 5.0.

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Section: Discussionmentioning

confidence: 99%

Purification and Characterization of an Oat Fructan Exohydrolase That Preferentially Hydrolyzes [beta]-2,6-Fructans

Henson

Livingston

1996

Plant Physiol.

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“…For example, inulinases and levanases are capable of hydrolyzing inulin; levan and sucrose have been isolated from Bacillus subtilis (29), Actinomyces viscosus ATCC 15987 (33), S. mutans (9), Saccharomyces fragilis (45), and Chrysosporium pannorum (54). Enzymes active for inulin and sucrose but not levan are found in filamentous fungi among the ␤-fructofuranosidases (I to III) from A. niger (52) and C. pannorum (54), However, levanases which are specific for levan have been isolated from S. salivarius and Actinomyces viscosus ATCC 19246 (2). Here, we show that the exo-inulinase from S. salivarius ATCC 9759 has similar functions to the exoinulinase from A. niger in addition to being a levanase.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Streptococcus mutans Biofilm Formation by Streptococcus salivarius FruA

Ogawa

Furukawa

Fujita

et al. 2011

Appl Environ Microbiol

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The oral microbial flora consists of many beneficial species of bacteria that are associated with a healthy condition and control the progression of oral disease. Cooperative interactions between oral streptococci and the pathogens play important roles in the development of dental biofilms in the oral cavity. To determine the roles of oral streptococci in multispecies biofilm development and the effects of the streptococci in biofilm formation, the active substances inhibiting Streptococcus mutans biofilm formation were purified from Streptococcus salivarius ATCC 9759 and HT9R culture supernatants using ion exchange and gel filtration chromatography. Matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry analysis was performed, and the results were compared to databases. The S. salivarius HT9R genome sequence was determined and used to indentify candidate proteins for inhibition. The candidates inhibiting biofilms were identified as S. salivarius fructosyltransferase (FTF) and exo-beta-D-fructosidase (FruA). The activity of the inhibitors was elevated in the presence of sucrose, and the inhibitory effects were dependent on the sucrose concentration in the biofilm formation assay medium. Purified and commercial FruA from Aspergillus niger (31.6% identity and 59.6% similarity to the amino acid sequence of FruA from S. salivarius HT9R) completely inhibited S. mutans GS-5 biofilm formation on saliva-coated polystyrene and hydroxyapatite surfaces. Inhibition was induced by decreasing polysaccharide production, which is dependent on sucrose digestion rather than fructan digestion. The data indicate that S. salivarius produces large quantities of FruA and that FruA alone may play an important role in multispecies microbial interactions for sucrose-dependent biofilm formation in the oral cavity.

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“…The first group, the unspecific /?-D-fructofuranosidases (^-D-fructan-fructohydrolase, EC 3 .2.1.80 and /6'-D-fructofuranosidefructohydrolase, EC 3 .2.1.26) hydrolyse the terminal unsubstituted fructose residue from the fructan chain. Many of these enzymes hydrolyse levan, inulin, sucrose, raffinose and stachyose but there are differences in substrate specificity and affinity (Dacosta & Gibbons, 1968;Xiao, Tanida & Takao, 1989 Bacillus, Clostridium, Bacteroides). For the most part, the /?-2,6 hydrolytic properties of these enzymes have not been tested (Manzoni & Cavazzoni, 1991;Belamri et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Purification and substrate specificity of an extracellular fructanhydrolase from Lactobacillus paracasei ssp. paracasei P 4134

MÜLLER

SEYFARTH

1997

New Phytologist

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SUMMARYA novel extracellular fructanhydrolase was isolated from the culture filtrate of Lactobacillus paracasei ssp. paracasei P4134 grown on a mineral medium supplemented with fructan extracted from Timothy {Phleum pratense L.) as the only carbon source. The enzyme was purified by a combination of ammonium sulphate precipitation, affinity chromatography, preparative isoelectric focusing and anion-exchange chromatography. As a result of these procedures, the specific enzyme activity increased 93-fold, with a final yield of 28-4%. The substrate-specific activities against different fructan types were determined by incubating the enzyme fractions with fructan extracted from Timothy (predominantly /5-2,6 fructosyl-fructose linkages), inulin from Dahlia tubers (mostly /?-2,l fructosyl-fructose linkages) and sucrose. The purified enzyme catalysed the hydrolysis of /?-2,6-linked fructan more rapidly than the /?-2,l linkages of inulin. Additionally, the enzyme showed low ability to hydrolyse sucrose. Fructose was the main product of the degradation of Timothy fructan and inulin, indicating a high exohydrolytic activity of the enzyme. It is proposed that the fructan-degrading enzyme from L. paracasei ssp. paracasei P 4134 is a /?-D-fructan-fructohydrolase (EC 3.2.1.80). The enzyme preparation showed a single protein band in sodium dodecyl sulphate-polyacrylamide gel electrophoresis with a mobility corresponding to molecular weight of c. 42 kDa. It was concluded that only one molecular weight of fructan-degrading enzyme exists in L. paracasei ssp. paracasei P 4134.

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Purification and characteristics of two exoinulinases from Chrysosporium pannorum

Cited by 29 publications

References 13 publications

Purification and Characterization of an Oat Fructan Exohydrolase That Preferentially Hydrolyzes [beta]-2,6-Fructans

Purification and Characterization of an Oat Fructan Exohydrolase That Preferentially Hydrolyzes [beta]-2,6-Fructans

Inhibition of Streptococcus mutans Biofilm Formation by Streptococcus salivarius FruA

Purification and substrate specificity of an extracellular fructanhydrolase from Lactobacillus paracasei ssp. paracasei P 4134

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