Citation
Ariff, Arbakariya and Mohamad, Rosfarizan and Ghani, B. and Sugio, Tsuyoshi and Abdul Karim, Mohamed Ismail
(1997)
Molybdenum reductase in Enterobacter cloacae.
World Journal of Microbiology and Biotechnology, 13 (6).
pp. 643-647.
ISSN 0959-3993; ESSN: 1573-0972
Abstract
Under anaerobic conditions in glucose–yeast extract medium with phosphate, Enterobacter cloacae strain 48 grew well and reduced Mo6+, to Mo5+. The activity of Mo6+-reductase was measured by the formation of molybdenum blue (complexation between Mo5+ and phosphate ion). Models based on logistic and Luedeking–Piret equations were found adequate to describe the growth of E. cloacae and Mo6+-reductase production. Mo6+-reductase production was found to be a growth-associated process. Washed intact cells, membrane fraction (after disruption using a sonicator) and fluid supernatant (after cell disruption) were able to reduce Mo6+. However, Mo6+-reductase activity was much lower in the supernatant fluid. The (NH4)2SO4-precipitated Mo6+-reductase extract from fluid supernatant was assayed for its properties. The optimum pH and temperature for Mo6+-reductase activity were 8 and 30°C, respectively. The apparent Michaelis–Menten constant (Km) and a maximum velocity (Vmax) were 16.5mm and 0.0192μmol/ml.h, respectively.
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