Heat-set gelation of milk- and fermentation-derived β-lactoglobulin variants
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Date
2025-08
Open Access Location
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier Ltd
Rights
(c) 2025 The Author/s
CC BY 4.0
CC BY 4.0
Abstract
Milk-derived β-lactoglobulin (mβ-LG) and fermentation-derived β-lactoglobulin (fβ-LG) may slightly differ in their amino acid sequences. This study aims to investigate the heat-set gelling behaviour of mβ-LG (variants A, B, and C) and fβ-LG A variants. Differential scanning calorimetry indicated similar denaturation temperatures for mβ-LG A and fβ-LG A (∼75 °C), with mβ-LG C highest (∼81 °C) and mβ-LG B intermediate (∼78 °C). All fβ-LG A formed translucent gels with a fine-stranded structure, whereas mβ-LG A, B, and C formed opaque gels with a coarse particulate structure. fβ-LG A exhibited delayed gelation onset and lower gel stiffness compared to mβ-LG A. Among mβ-LG's, mβ-LG A showed the highest gel stiffness, followed by mβ-LG B and then mβ-LG C. Rheological analysis showed that fβ-LG A gels were more elastic and ductile compared to mβ-LG A gels, indicated by smaller tan δ values and delayed increases in energy dissipation ratio at higher strain amplitude; mβ-LG B and mβ-LG C gels were less elastic but more ductile compared to mβ-LG A gels. The more elastic and ductile nature of fβ-LG A gels indicates their potential for applications requiring these specific textural properties. By selecting mβ-LG variants from milk and/or utilizing precision fermentation to engineer additional differences, it is possible to tailor the gelation characteristics of β-LG to meet specific functional requirements.
Description
Keywords
Precision fermentation, β-Lactoglobulin, Genetic variants, Amino acid sequence, Rheology, LAOS
Citation
Pan Z, Kornet R, Hewitt S, Welman A, Hill JP, Wubbolts M, Mitchell S, McNabb WC, Ye A, Acevedo-Fani A, Anema SG. (2025). Heat-set gelation of milk- and fermentation-derived β-lactoglobulin variants. Food Hydrocolloids. 165.