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Updated: Oct 25, 2025

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Trace the difference driven by unfolding-refolding pathway of myofibrillar protein: Emphasizing the changes on
Liyuan Li1, Xue Zhao1, Xinglian Xu1
1College of Food Science and Technology, Key Laboratory of Animal Origin Food Production and Safety Guarantee of Jiangsu Province, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Joint International Research Laboratory of Animal Health and Food Safety, National Experimental Teaching Demonstration Center of Animal Science, Nanjing Agricultural University, Nanjing 210095, PR China.
Abstract:
The effective strategy of pH-shifting to improve the emulsifying properties of myofibrillar proteins (MPs) extracted from pale, soft and exudative (PSE)-like chicken was investigated. To determine the mechanism of improvement, changes on structural and physicochemical properties were clarified by tracing the difference driven by unfolding-refolding process. According to the results of tryptophan fluorescence intensity and circular dichroism spectroscopy, it is found that unfolding-refolding process markedly changed MPs secondary and tertiary structure. The atomic force microscopy images showed MPs appeared to have fibrous-like appearance at pH 7.0, however, exhibited as spherical shape after pH-shifting. Both emulsifying activity index and emulsifying stability index increased after pH-shifting. These results systematically illustrated the changes on structural and emulsion properties of MPs during unfolding-refolding process. It proved that the strategy pH 11.0-7.0 could more effectively promote MPs emulsifying properties, whose mechanism was simultaneously the transformation in MPs structure and potentially formation of highly-soluble particle.
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