Abstract

Aspergillus sp. phytase contains five disulfide bonds. In order to elucidate their role, the reactivation and refolding of phytase in the absence and presence of dithiothreitol (DTT) was investigated. The results indicated that the disulfide bonds play an important role in the catalytic activity and conformational stability of the enzyme.

Keywords: phytase, refolding, disulfide bond, conformational stability, enzyme activity