Influence of Disulfide Bonds on the Conformational Changes and Activities of Refolded Phytase

Title: Influence of Disulfide Bonds on the Conformational Changes and Activities of Refolded Phytase

Volume: 12 Issue: 6

Author(s): G. Y. Song, X. Y. Wang and M. Wang

Affiliation:

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

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.

Cite this article as:

Song Y. G., Wang Y. X. and Wang M., Influence of Disulfide Bonds on the Conformational Changes and Activities of Refolded Phytase, Protein & Peptide Letters 2005; 12 (6) . https://dx.doi.org/10.2174/0929866054395752

DOI https://dx.doi.org/10.2174/0929866054395752	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305