Production of a thermostable ATPase by the facultative thermophile,Bacillus coagulans
โ Scribed by C. Edwards; M. V. Jones
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 267 KB
- Volume
- 135
- Category
- Article
- ISSN
- 0302-8933
No coin nor oath required. For personal study only.
โฆ Synopsis
The properties of the ATPase in the facultative thermophile, Bacillus coagulans, grown at thermophilic or mesophilic temperatures were similar. Arrhenius plots did not show discontinuities indicative of thermoadaptation. Magnesium stimulation of the enzyme was dependant on the assay temperature but independant of the growth temperature. The ATPase in cells grown at 35~ or 55~ was equally thermostable at 65~
In contrast, the ATPase from the mesophile, Bacillus megaterium (Tma x = 42 ~ C) was completely inactivated at 55~ in 5min.
๐ SIMILAR VOLUMES
The Azorobucrer-type 7Fe ferredoxin from Bacillus schlegelii was active as an electron carrier in the reduction system of cyt. c consisting of NADPH, FNR and cytochrome c (cyt. c). The only [ 3Fe\_4S] cluster in the Fd molecule acts as the active site for the reduction of cyt. c. The activity of the
We describe the use of a thermostable glucokinase in a novel competitive fluorescence assay for glucose. Glucokinase from Bacillus stearothermophilus (BSGK) was found to retain enzymatic activity in solution for over 20 days. The single cysteine residue in BSGK, which is near the active site, was la