Pentose Metabolism inClostridium acetobutylicum

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Abstract
L-Arabinose ketol-isomerase (EC 5.3.1.4) was extracted from the l-arabinose-grown cells of Clostridium acetobutylicum and partially purified by ammonium sulfate fractionation, DEAE-cellulose column chromatography and the gel filtration on Sephadex G–200. Optimum pH and temperature for the activity of the enzyme were 7.5 and 37°C, respectively. The enzyme was inhibited by EDTA, Na-pyrophosphate and KCN, and its activity was restored by the addition of divalent metal ions such as Mn2+ and Co2+. The Michaelis-Menten’s constants for l-arabinose, Mn2+ and Co2+ were 1.08 × 10−2 m, 0.83 × 10−4 m and 0.38 ×10−4m, respectively. The equilibrium constant (K = ribulose/arabinose) was 3.14 (37°C, pH 7.5). The thermodynamic quantities, ∆H, ∆G (37°C), ∆S (37°C) and E were +7354 cal/mole, − 710.7 cal/mole, +26.0 cal/(deg·mole) and +7471 cal/mole, respectively.

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