Phosphorolytic cleavage of sucrose by sucrose-grown ruminal bacterium Pseudobutyrivibrio ruminis strain k3
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
- MeSH
- bachor mikrobiologie MeSH
- bakteriální proteiny chemie izolace a purifikace metabolismus MeSH
- chromatografie na tenké vrstvě MeSH
- fosfáty metabolismus MeSH
- fruktosa metabolismus MeSH
- glukosafosfáty metabolismus MeSH
- glukosyltransferasy chemie izolace a purifikace metabolismus MeSH
- grampozitivní bakterie izolace a purifikace metabolismus MeSH
- kinetika MeSH
- koncentrace vodíkových iontů MeSH
- kultivační média chemie MeSH
- molekulová hmotnost MeSH
- sacharosa metabolismus MeSH
- stabilita enzymů MeSH
- teplota MeSH
- uhlík metabolismus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- fosfáty MeSH
- fruktosa MeSH
- glucose-1-phosphate MeSH Prohlížeč
- glukosafosfáty MeSH
- glukosyltransferasy MeSH
- kultivační média MeSH
- sacharosa MeSH
- sucrose phosphorylase MeSH Prohlížeč
- uhlík MeSH
Rumen bacterium Pseudobutyrivibrio ruminis strain k3 utilized over 90% sucrose added to the growth medium as a sole carbon source. Zymographic studies of the bacterial cell extract revealed the presence of a single enzyme involved in sucrose digestion. Thin layer chromatography showed fructose and glucose-1-phosphate (Glc1P) as end products of the digestion of sucrose by identified enzyme. The activity of the enzyme depended on the presence of inorganic phosphate and was the highest at the concentration of phosphate 56 mmol/L. The enzyme was identified as the sucrose phosphorylase (EC 2.4.1.7) of molar mass approximately 54 kDa and maximum activity at pH 6.0 and 45 degrees C. The calculated Michaelis constant (Km) for Glc1P formation and release of fructose by partially purified enzyme were 4.4 and 8.56 mmol/L while the maximum velocities of the reaction (Vlim) were 1.19 and 0.64 micromol/L per mg protein per min, respectively.
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