earticle

영어

Thermostabilization of enzymes has been a key research topic because it industrially gives a number of beneficial advantages. Among various strategies to increase thermostability of enzymes, enhancement of residual packing at the core of an enzyme structure is commonly accepted as a successful strategy. Applying this strategy to Bacillus subtilis lipase A, its thermostability is increased, however, its activity is simultaneously decreased. In this study, rational packing strategy for minimizing loss of enzyme activity is proposed. Enzyme activity is usually decreased by conformational change at the catalytic site. Previous packing strategy is
generally accompanied with conformational change because it does not consider space for mutated residues. The hypothesis of this study is that residual packing at the empty space should minimize conformational change and prevent loss of enzyme activity. To demonstrate this hypothesis, residual packing space for Bacillus subtilis lipase A was calculated. The
results show that there is not enough space for mutated residues and this is the reason why its activity was decreased as it caused conformational change. In conclusion, this rational packing strategy can be widely used to enzymes to enhance thermostability of enzymes without loss of its activity.