Open AccessProperties of the ATP phosphohydrolase of the facultative thermophile Bacillus coagulans
Author(s) -
Ball A.,
Edwards C.,
Jones M.V.
Publication year - 1985
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1985.tb00656.x
Subject(s) - thermostability , facultative , bacillus coagulans , thermophile , enzyme , fractionation , bacillus cereus , biochemistry , differential centrifugation , bacillales , centrifugation , bacillus (shape) , biology , specific activity , membrane , bacteria , chemistry , microbiology and biotechnology , chromatography , fermentation , botany , genetics , bacillus subtilis
Abstract The thermostability of the ATP phosphohydrolase of the facultative thermophile Bacillus coagulans has been investigated. Fractionation of disintegrated cell suspensions by differential centrifugation revealed a similar distribution of enzyme activity irrespective of growth temperature. Most of the activity was located in the membrane fraction. Thermostability of solubilized (BF 1 ) preparation from cells grown at 37°C or 55°C was similar, but membrane‐bound BF 0 BF 1 from 37°C‐grown cells was inactivated at lower temperatures than that from 55°C‐grown cells. Inhibition of the membrane‐bound (BF 0 BF 1 )ATPase by 4‐chloro‐7‐nitro‐benzofuran (NbfCl) and quercetin, which both act on the BF 1 portion of the enzyme, was different from that seen with the soluble (BF 1 ) enzyme. The results show that some modification of BF 1 must occur when the enzyme is membrane‐bound.