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Purification and properties of two fructose-6-phosphate phosphoketolases inBifidobacterium

✍ Scribed by B. Sgorbati; G. Lenaz; F. Casalicchio

Book ID
104757480
Publisher
Springer Netherlands
Year
1976
Tongue
English
Weight
464 KB
Volume
42
Category
Article
ISSN
0003-6072

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✦ Synopsis

Fructose-6-phosphate phosphoketolase was purified from type strains of two species of the genus Bifidobaeterium: B. globosum and B. dentium. The first species has a preferred "animal" habitat, like feces of animals and rumen of cattle; the latter is harboured in "human" habitats, like feces and dental caries of man. Two electrophoretic types of phosphoketolase (F6PPK) were previously distinguished and called "animal" and "human" type according to the habitat of the bifid organism. The purified preparations of these two phosphoketolases displayed very different optimum pH range, metal activator and molecular weight; outstanding difference was found in the substrate specificity: the enzyme from B. globosum was able to split xylulose-5-P as well as fructose-6-P, whereas the phosphoketolase from B. dentium appeared to be specific for fructose-6-P.

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L-(+)-lactate dehydrogenase (LDH) from Staphylococcus epidermidis ATCC 14990 was purified by affinity chromatography. The purified enzyme was specifically activated by fructose-1,6-diphosphate (FDP). The concentration of FDP required for 50% maximal activity was about 0.15 mM. The enzyme activity wa