• Structural evolution of β-lact...

Treffer: Structural evolution of β-lactoglobulin under intensified magnetic fields.

Title:
Structural evolution of β-lactoglobulin under intensified magnetic fields.
Authors:
Chang X; College of Chemical Engineering, Inner Mongolia University of Technology, Hohhot 011500, China., Yue Y; China Inner Mongolia EHV Power Supply Bureau, Hohhot 010080, China., Lu Z; State Key Laboratory of Electrical Insulation and Power Equipment, Xi'an Jiaotong 9 University, Xi'an 710049, China., Tong Y; College of Chemical Engineering, Inner Mongolia University of Technology, Hohhot 011500, China., Li J; College of Chemical Engineering, Inner Mongolia University of Technology, Hohhot 011500, China., Hu Z; College of Chemical Engineering, Inner Mongolia University of Technology, Hohhot 011500, China., Yang L; State Key Laboratory of Electrical Insulation and Power Equipment, Xi'an Jiaotong 9 University, Xi'an 710049, China., Liu P; College of Chemical Engineering, Inner Mongolia University of Technology, Hohhot 011500, China. Electronic address: lpl1023@imut.edu.cn.
Source:
Food research international (Ottawa, Ont.) [Food Res Int] 2026 Jan 15; Vol. 223 (Pt 2), pp. 117856. Date of Electronic Publication: 2025 Nov 13.
Publication Type:
Journal Article
Language:
English
Journal Info:
Publisher: Published on behalf of the Canadian Institute of Food Science and Technology by Elsevier Applied Science Country of Publication: Canada NLM ID: 9210143 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-7145 (Electronic) Linking ISSN: 09639969 NLM ISO Abbreviation: Food Res Int Subsets: MEDLINE
Imprint Name(s):
Original Publication: Ottawa, Ontario, Canada : Published on behalf of the Canadian Institute of Food Science and Technology by Elsevier Applied Science, c1992-
MeSH Terms:
Lactoglobulins*/chemistry , Magnetic Fields*, Particle Size ; Emulsions ; Oxidation-Reduction ; Protein Structure, Secondary ; Protein Folding ; Protein Stability ; Protein Conformation
Contributed Indexing:
Keywords: Aggregate; Magnetic field; Properties; Structure; β-lactoglobulin
Substance Nomenclature:
0 (Lactoglobulins)
0 (Emulsions)
Entry Date(s):
Date Created: 20251208 Date Completed: 20251208 Latest Revision: 20251208
Update Code:
20251209
DOI:
10.1016/j.foodres.2025.117856
PMID:
41360548
Database:
MEDLINE

Weitere Informationen

This study investigates the structural and functional changes of β-lactoglobulin (β-LG) under incremental magnetic fields (IMF: 5, 10, 15, 20 T). Multi-scale characterization reveals four stages of conformational transition: contraction (5 T), folded compaction (10 T), aggregation/refolding (15 T), and unfolding/etching (20 T). The magnetic field was found to induce ordering of the secondary structure and promote oxidation reactions among CC, C-O-C, and O-C=O groups, thereby enhancing the crystallinity, emulsifying properties, and freeze-thaw stability of β-LG. Notably, at 10 T, the particle size reached a minimum of 67.46 ± 2.33 μm, representing a 32.23 % reduction (p < 0.05). The secondary structure showed increased order, with α-helix and β-sheet contents of 7.45 % and 58.74 %, respectively. Functional properties were optimized at 10 T: emulsifying activity increased to 10.26 m <sup>2</sup> /g (a 34.82 % improvement) and emulsifying stability to 81.70 % (a 72.04 % improvement), while freeze-thaw water precipitation was reduced by 15.4 %. These results fully demonstrate that IMF can precisely restructure β-LG through oxidative folding-unfolding transitions, establishing 10 T as the critical magnetic field strength for enhancing functionality in dairy and bioactive delivery applications.
(Copyright © 2024. Published by Elsevier Ltd.)

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.