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Citation: XIAO Hou-Rong, XU Xiao-Long, XIE Yong-Shu, LIU Qing-Liang. Renaturation of GdnHCl-denatured Polyphenol Oxidase from Tobacco[J]. Chinese Journal of Applied Chemistry, ;2005, 22(1): 9-13. shu

Renaturation of GdnHCl-denatured Polyphenol Oxidase from Tobacco

1.
Department of Chemistry, University of Science and Technology of China, Hefei 230026

Corresponding author: LIU Qing-Liang,
Received Date: 14 May 2004
Available Online: 10 July 2004
Fund Project: 国家自然科学基金资助项目(30270321) (30270321)

The renaturation of polyphenol oxidase from Tobacco denatured in 6.0 mol/L guanidine hydrochloride(GdnHCl) was investigated. In the absence of additives(s), the optimal renaturation conditions, with 63.36% of activity recovered, are as follows:1.5 mol/L GdnHCl, denaturation time 30 min, renaturation temperature 4℃ and enzyme concentration 1.5×10^-4 g/mL. 1.0 mol/L (NH₄)₂SO₄ showed a limited effect on the recovering of PPO activity. Using both 1.0 mol/L (NH₄)₂SO₄ and 100 μmol/L CuSO₄ was the most effective method, and the renaturation system with both CTAB and β-CD together showed a more favorable effect on the enzyme renaturation, than that with the single β-CD.
- polyphenol oxidase,
- renaturation,
- guanidine hydrochloride,
- β-cyclodextrin,
- cetyl trimethylammo nium bromide
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