Molybdenum reductase in Enterobacter cloacae
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 L...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English English |
| Published: |
Rapid Science Publishers
1997
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| Online Access: | http://psasir.upm.edu.my/id/eprint/51047/1/51047.pdf http://psasir.upm.edu.my/id/eprint/51047/7/A_1018562719751.pdf http://psasir.upm.edu.my/id/eprint/51047/ http://rd.springer.com/article/10.1023/A:1018562719751 |
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| Institution: | Universiti Putra Malaysia |
| Language: | English English |
| Summary: | 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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