Author/Authors :
vchinnikova, M.V Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry - Russian Academy of Sciences, Moscow, Russia , Mikhailova, A.G Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry - Russian Academy of Sciences, Moscow, Russia , Karlinsky, D.M Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry - Russian Academy of Sciences, Moscow, Russia , Gorlenko, V.A Moscow State Pedagogical University, Moscow, Russia , Rumsh, L.D Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry - Russian Academy of Sciences, Moscow, Russia
Abstract :
A unique property was found for oligopeptidase B from Serratia proteamaculans (PSP) as well as its mutants: they can undergo reversible thermal inactivation at 37°C, with activity being restored or even increased with respect to the initial one upon subsequent cooling. The process can be repeated several times, with the same results achieved (up to 5 cycles). This effect can be explained by a shift in the equilibrium between the inactive open form of the enzyme and the active closed one upon variation of the incubation temperature.
