Thermostability of Bacillus subtilis neutral protease.
The thermostability of the B. subtilis neutral protease was studied under various conditions. At elevated temperatures the enzyme was inactivated as a result of autolysis. The rate of inactivation did not depend on the enzyme concentration and the enzyme was most stable near its pH optimum. The rate of inactivation was unaffected by the presence of a second protease during the incubation at high temperatures. The results indicate that the rate of thermal inactivation of the neutral protease is determined by the kinetics of local unfolding processes that precede autolysis rather than by the catalytic rate of the autodigestion reaction or an irreversible unfolding step.
Eijsink
V G
VG
Department of Genetics, Centre of Biological Sciences, Haren, The Netherlands.
van den Burg
B
B
Vriend
G
G
Berendsen
H J
HJ
Venema
G
G
D001412:Bacillus subtilis / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D008666:Metalloendopeptidases / Q000737:chemistry*; D008956:Models, Chemical; D016297:Mutagenesis, Site-Directed; D011489:Protein Denaturation; D015202:Protein Engineering; D015032:Zinc / Q000737:chemistry
D008666:Metalloendopeptidases; C044194:microbial metalloproteinases; D015032:Zinc