High Temperature Increases the Refolding Yield of Reduced Lysozyme: Implication for the Productive Process for Folding | Zendy

Sakamoto Ryusuke | Zendy; Nishikori Shingo | Zendy; Shiraki Kentaro | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

High Temperature Increases the Refolding Yield of Reduced Lysozyme: Implication for the Productive Process for Folding

Author(s) -

Sakamoto Ryusuke,

Nishikori Shingo,

Shiraki Kentaro

Publication year - 2004

Publication title -

biotechnology progress

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.572

H-Index - 129

eISSN - 1520-6033

pISSN - 8756-7938

DOI - 10.1021/bp034385b

Subject(s) - protein folding , lysozyme , chemistry , yield (engineering) , folding (dsp implementation) , dilution , unfolded protein response , crystallography , biophysics , biochemistry , thermodynamics , biology , endoplasmic reticulum , physics , electrical engineering , engineering

Misfolding poses a serious problem in the biotechnological field in obtaining the active protein from inclusion bodies. Here we show that high temperature increases the refolding yield of reduced lyosyzme by a simple dilution method. The refolding yields at 98 °C were three times higher than those at 20 °C in the solutions tested, which is related to the fact that the thermally unfolded state of lysozyme is a more productive form for folding than the denaturant‐induced fully unfolded state. The thermal‐assisted refolding could be used for various reduced and denatured proteins as a result of its simplicity and low cost.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research