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

G.   Y.   Song; X.   Y.   Wang; M.      Wang

doi:10.2174/0929866054395752

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

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Protein & Peptide Letters

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

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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.

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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