Trace the difference driven by unfolding-refolding pathway of myofibrillar protein: Emphasizing the changes on structural and emulsion properties.
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Authors
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Li, Liyuan1
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Zhao, Xue2
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Xu, Xinglian3
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1
College 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.
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(China)
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2
College 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. Electronic address: [email protected]
,
(China)
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3
College 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. Electronic address: [email protected]
,
(China)
- Type
- Published Article
- Journal
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Food chemistry
- Publication Date
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Jan 15, 2022
- Volume
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367
- Pages
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130688–130688
- Identifiers
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DOI: 10.1016/j.foodchem.2021.130688
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PMID: 34365246
- Source
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Medline
- Keywords
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- Language
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English
- License
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Unknown
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. Copyright © 2021. Published by Elsevier Ltd.
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
This record was last updated on 01/04/2022 and may not reflect the most current and accurate biomedical/scientific data available from NLM.
The corresponding record at NLM can be accessed at
https://www.ncbi.nlm.nih.gov/pubmed/34365246
