Engineering de novo disulfide bond in bacterial α-type carbonic anhydrase for thermostable carbon sequestration.

ABSTRACT: Exploiting carbonic anhydrase (CA), an enzyme that rapidly catalyzes carbon dioxide hydration, is an attractive biomimetic route for carbon sequestration due to its environmental compatibility and potential economic viability. However, the industrial applications of CA are strongly hampered by the unstable nature of enzymes. In this work, we introduced in silico designed, de novo disulfide bond in a bacterial α-type CA to enhance thermostability. Three variants were selected and expressed in Escherichia coli with an additional disulfide bridge. One of the variants showed great enhancement in terms of both kinetic and thermodynamic stabilities. This improvement could be attributed to the loss of conformational entropy of the unfolded state, showing increased rigidity. The variant showed an

SUBMITTER: Jo BH 

PROVIDER: S-EPMC4935852 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature