Hydrolysis of milk oligosaccharides by the oral bacterium Streptococcus sanguis ATCC 10557

Shizukuishi, Satoshi; Nonaka, Hidemi; Nagata, Kiyoshi; Shibata, Satoaki; Nakamura, Ryô; Tsunemitsu, Akira

doi:10.1016/0003-9969(80)90157-0

Cited by 3 publications

(2 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…sanguis FSS2 grown in batch or continuous culture (Table 1) expresses a wide range of protease and glycosidase activities. Other S. sanguis group strains grown in batch or continuous culture also have displayed protease activities including arginine-, lysine-and tyrosine-peptidases (13,14,39), and glycosidase activities including neuraminidase, a-L-fucosidase, P-D-galactosidase, and A^-acetyl-P-D-glucosaminidase (42). However, the casein peptidase complex reported by Rogers et al (39) in S. sanguis P4A7 was not found in S. sanguis FSS2.…”

Section: Discussionmentioning

confidence: 96%

Modulation of glycosidase and protease activities by chemostat growth conditions in an endocarditis strain of Streptococcus sanguis

Mayo

Zhu

Harty

et al. 1995

Oral Microbiology and Immunology

View full text Add to dashboard Cite

The effects of growth conditions on the properties of the endocarditis-producing oral bacterium Streptococcus sanguis FSS2 were studied. This strain produces a variety of proteases and glycosidases, including a thrombin-like activity that is a potential virulence factor for endocarditis. Cultures were grown with limiting glucose or galactose in chemostats over a range of dilution rates and pH levels, and the following activities were measured at pH 7.5: thrombin-like, Hageman factor-like, N-acetyl-beta-D-galactosaminidase, beta-D-glucosidase, and beta-D-galactosidase. At growth pH 6.5, specific activities generally decreased as the dilution rate increased from 0.05 to 0.40 h(-1). At a dilution rate of 0.1 h(-1), specific activities generally were highest at growth pH 6.5 and lower and approximately equal at growth pH 5.5 and 7.5. The major exception was the thrombin-like activity, for which the specific activity at growth pH 7.5 was approximately 5-fold higher than at growth pH 5.5. Hageman factor-like activity was apparently glucose catabolite repressible, as its activity was 3-fold higher in galactose cultures. The measured activities changed as functions of growth conditions and thus were modulated by environment. Environmental regulation of thrombin-like activity by pH is consistent with an activity that is less important on tooth surfaces than in tissues.

show abstract

Section: Discussionmentioning

confidence: 96%

Modulation of glycosidase and protease activities by chemostat growth conditions in an endocarditis strain of Streptococcus sanguis

Mayo

Zhu

Harty

et al. 1995

Oral Microbiology and Immunology

View full text Add to dashboard Cite

show abstract

“…The percentage specifically bound was calculated by dividing cpm specifically eluted by total cpm recovered. In most cases, assays were run at 4°C to decrease the potential for bacterial enzyme activity [18,19]. When bacteria could not be eluted at 4°C, bacterial enzymes were inactivated by heat and the assay was run at 22°C.…”

Section: Whole Cell Affinity Chromatographymentioning

confidence: 99%

The identification of oral microbial lectins by cell affinity chromatography

Murray

Materese

Hoover

et al. 1987

FEMS Microbiology Letters

View full text Add to dashboard Cite

Whole‐cell affinity chromatography was used as a novel screening technique for identifying and characterizing oral microbial lectins. First, affinity columns bearing oligosaccharides of defined structure were synthesized as lectin‐binding reagents. Fetuin, transferrin (containing terminal NeuAc residues), asialofetuin and asialotransferrin (with terminal Gal residues) were covalently coupled to Sepharose 6MB and incubated with 3H‐labeled bacterial suspensions in columns fitted with an 80‐μm nylon filter. Bacteria specifically bound were then eluted with the appropriate sugar (NeuAc or Gal). Fusobacterium nucleatum was the most significant binder, with 80% specifically eluted from the asialo‐derivatives. Actinomyces viscosus and Actinomyces naeslundii also showed unique specificity for galactose. In contrast, Streptococcus sanguis bound in greatest numbers to fetuin, consistent with the presence of a sialic acid‐binding site on these bacteria.

show abstract

Utilization of mucin by oral Streptococcus species

Hoeven

Kieboom

Camp

1990

Antonie van Leeuwenhoek

View full text Add to dashboard Cite

The ability of oral Streptococcus strains to utilize oligosaccharide chains in mucin as a source of carbohydrate was studied in batch cultures. Pig gastric mucin, as a substitute of human salivary mucin, was added to chemically defined medium containing no other carbohydrates. Strains of S. mitior attained the highest cell density, while mutans streptococci: S. mutans, S. sobrinus, S. rattus, grew very little in the medium with mucin. S. mitis, S. sanguis, and S. milleri in decreasing order, showed intermediate growth. Mucin breakdown as measured by sugar analyses indicated that oligosaccharide chains were only partially degraded. Every strain produced one or more exoglycosidases potentially involved in hydrolysis of oligosaccharide. The enzyme activities occurred mainly associated with the cells, and very little activity was found in the culture fluids. The relationships between glycosidase activities and growth, or mucin degradation were not always clear.

show abstract

Hydrolysis of milk oligosaccharides by the oral bacterium Streptococcus sanguis ATCC 10557

Cited by 3 publications

References 9 publications

Modulation of glycosidase and protease activities by chemostat growth conditions in an endocarditis strain of Streptococcus sanguis

Modulation of glycosidase and protease activities by chemostat growth conditions in an endocarditis strain of Streptococcus sanguis

The identification of oral microbial lectins by cell affinity chromatography

Utilization of mucin by oral Streptococcus species

Contact Info

Product

Resources

About