Back to Search
Start Over
Comparison and analysis of mechanism of β-lactoglobulin self-assembled gel carriers formed by different gelation methods.
- Source :
-
Food chemistry [Food Chem] 2024 Jun 01; Vol. 442, pp. 138414. Date of Electronic Publication: 2024 Jan 14. - Publication Year :
- 2024
-
Abstract
- Based on the findings of our previous studies, a comprehensive comparative investigation of the quality and formation mechanism of gels obtained from protein self-assemblies induced by different methods is necessary. Self-assembled heat-induced gels had higher gel mechanical strength, and hydrophobic interactions played a greater role. Whether or not heat treatment was used to induce gel formation may play a more important role than the effect of divalent cations on gel formation. Hydrogen bonds played an important role in all gels formed using different gelation methods. Furthermore, Self-assembled cold-induced gels were considered to can load bioactive substances with different hydrophilicity properties due to the high water-holding capacity and the smooth, dense microstructure. Therefore, β-lactoglobulin fibrous and worm-like self-assembled cold-induced gels as a delivery material for hydrophilic bioactive substances (epigallocatechin gallate, vitamin B <subscript>2</subscript> ) and amphiphilic bioactive substance (naringenin), with good encapsulation efficiency (91.92 %, 97.08 %, 96.72 %, 96.52 %, 98.94 %, 97.41 %, respectively) and slow-release performance.<br />Competing Interests: 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.<br /> (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Subjects :
- Gels chemistry
Hot Temperature
Lactoglobulins chemistry
Water chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1873-7072
- Volume :
- 442
- Database :
- MEDLINE
- Journal :
- Food chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 38237299
- Full Text :
- https://doi.org/10.1016/j.foodchem.2024.138414