Enzymatic properties of atrazine chlorohydrolase entrapped in biomimetic silica

Abstract

Purified atrazine chlorohydrolase (AtzA) was entrapped in the nanoparticles of biomimetically synthesized silica at the ambient condition within 20 min. Entrapped AtzA in biomimetic silica was less affected by pH change and showed higher thermostability than free enzymes. The entrapped AtzA was also more tolerant against proteolysis, with 80% of the initial activity remaining and retained 82% of the initial activity even after four cycles of usage. These results suggest that entrapment of AtzA in biomimetic silica could be utilized under diverse environmental conditions with the active catalytic performance sustained.