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

ISSN: 0929-8665
E-ISSN: 1875-5305

Influence of Disulfide Bonds on the Conformational Changes and Activities of Refolded Phytase
Authors: G. Y. Song¹, X. Y. Wang² and M. Wang³
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¹ College of Life Science, Shandong Agricultural University, Shandong Tai'an 271018, People's Republic of China. ² College of Life Science, Shandong Agricultural University, Shandong Tai'an 271018, People's Republic of China. ³ College of Life Science, Shandong Agricultural University, Shandong Tai'an 271018, People's Republic of China.
Source: Protein and Peptide Letters, Volume 12, Issue 6, Aug 2005, p. 533 - 535
DOI: https://doi.org/10.2174/0929866054395752
- Available online: 01 Aug 2005

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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2005-08-01

2025-09-01

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Article Type: Review Article

Keyword(s): conformational stability; disulfide bond; enzyme activity; phytase; refolding

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

Abstract

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