Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes
Bovine milk beta-lactoglobulin (BLG) is a small whey protein that is a common ingredient in many foods. Many of the properties of BLG relevant to the food industry are related to its unfolding processes induced by physical or chemical treatments. Unfolding occurs through a number of individual steps...
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| Format: | Article |
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MDPI AG
2022-02-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/27/3/1131 |
| _version_ | 1797485875850903552 |
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| author | Alberto Barbiroli Stefania Iametti Francesco Bonomi |
| author_facet | Alberto Barbiroli Stefania Iametti Francesco Bonomi |
| author_sort | Alberto Barbiroli |
| collection | DOAJ |
| description | Bovine milk beta-lactoglobulin (BLG) is a small whey protein that is a common ingredient in many foods. Many of the properties of BLG relevant to the food industry are related to its unfolding processes induced by physical or chemical treatments. Unfolding occurs through a number of individual steps, generating transient intermediates through reversible and irreversible modifications. The rate of formation of these intermediates and of their further evolution into different structures often dictates the outcome of a given process. This report addresses the main structural features of the BLG unfolding intermediates under conditions that may facilitate or impair their formation in response to chemical or physical denaturing agents. In consideration of the short lifespan of the transient species generated upon unfolding, this review also discusses how various methodological approaches may be adapted in exploring the process-dependent structural modifications of BLG from a kinetic and/or a thermodynamic standpoint. Some of the conceptual and methodological approaches presented and discussed in this review can provide hints for improving the understanding of transient conformers formation by proteins present in other food systems, as well as when other physical or chemical denaturing agents are acting on proteins much different from BLG in complex food systems. |
| first_indexed | 2024-03-09T23:26:02Z |
| format | Article |
| id | doaj.art-1cfd3db36df84260add1c56607db6886 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T23:26:02Z |
| publishDate | 2022-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-1cfd3db36df84260add1c56607db68862023-11-23T17:18:04ZengMDPI AGMolecules1420-30492022-02-01273113110.3390/molecules27031131Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding ProcessesAlberto Barbiroli0Stefania Iametti1Francesco Bonomi2Department of Food, Environmental and Nutritional Sciences (DeFENS), Università degli Studi di Milano, Via G. Celoria 2, 20133 Milan, ItalyDepartment of Food, Environmental and Nutritional Sciences (DeFENS), Università degli Studi di Milano, Via G. Celoria 2, 20133 Milan, ItalyDepartment of Food, Environmental and Nutritional Sciences (DeFENS), Università degli Studi di Milano, Via G. Celoria 2, 20133 Milan, ItalyBovine milk beta-lactoglobulin (BLG) is a small whey protein that is a common ingredient in many foods. Many of the properties of BLG relevant to the food industry are related to its unfolding processes induced by physical or chemical treatments. Unfolding occurs through a number of individual steps, generating transient intermediates through reversible and irreversible modifications. The rate of formation of these intermediates and of their further evolution into different structures often dictates the outcome of a given process. This report addresses the main structural features of the BLG unfolding intermediates under conditions that may facilitate or impair their formation in response to chemical or physical denaturing agents. In consideration of the short lifespan of the transient species generated upon unfolding, this review also discusses how various methodological approaches may be adapted in exploring the process-dependent structural modifications of BLG from a kinetic and/or a thermodynamic standpoint. Some of the conceptual and methodological approaches presented and discussed in this review can provide hints for improving the understanding of transient conformers formation by proteins present in other food systems, as well as when other physical or chemical denaturing agents are acting on proteins much different from BLG in complex food systems.https://www.mdpi.com/1420-3049/27/3/1131beta-lactoglobulinunfolding intermediatesimmunoreactivityfolding stabilityligands |
| spellingShingle | Alberto Barbiroli Stefania Iametti Francesco Bonomi Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes Molecules beta-lactoglobulin unfolding intermediates immunoreactivity folding stability ligands |
| title | Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes |
| title_full | Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes |
| title_fullStr | Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes |
| title_full_unstemmed | Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes |
| title_short | Beta-Lactoglobulin as a Model Food Protein: How to Promote, Prevent, and Exploit Its Unfolding Processes |
| title_sort | beta lactoglobulin as a model food protein how to promote prevent and exploit its unfolding processes |
| topic | beta-lactoglobulin unfolding intermediates immunoreactivity folding stability ligands |
| url | https://www.mdpi.com/1420-3049/27/3/1131 |
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