Streptavidin mutants

特許 権利維持 Most attempts at mutating streptavidin result in a lowered biotin-binding affinity, which is to be expected in such a highly optimised system. However, a recently engineered mutant of streptavidin, named traptavidin, was found to have more than ten-fold slower biotin dissociation, in addition to higher thermal and mechanical stability,[5] distributed by Oxford University Department of Biochemistry. This decreased dissociation rate was accompanied by a two-fold decrease in the association rate.