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. 1983 Oct;42(1):231–236. doi: 10.1128/iai.42.1.231-236.1983

Isolation and properties of levanase from Streptococcus salivarius KTA-19.

N Takahashi, F Mizuno, K Takamori
PMCID: PMC264548  PMID: 6618666

Abstract

Fructan-hydrolyzing enzyme from Streptococcus salivarius KTA-19 isolated from human dental plaque was investigated. The enzyme was purified by ammonium sulfate precipitation, acetone fractionation, and column chromatography on Bio-Gel and DEAE-cellulose. The purified enzyme showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing. Its molecular weight was 100,000 as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme exhibited an optimum pH of 6.5 and decreased its activity from pH 6.0 and especially below pH 5.5. The optimum temperature was 40 to 50 degrees C, and enzyme activity was reduced by 90% at 55 degrees C. Enzyme activity was markedly inhibited by Hg2+, Ag+, Cu2+, and p-chloromercuribenzoate at a concentration of 10(-3) M, but not by other metal ions or chemical effectors. Fructose was the only by-product of the enzyme action on levan. These results indicated that the levanase of S. salivarius KTA-19 is an exo-beta-(2,6)-fructofuranosidase.

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Selected References

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