Title
Stabilization of beta-lactoglobulin by polyols and sugars against temperature-induced denaturation involves diverse and specific structural regions of the protein
Author
Barbiroli, A.
Marengo, M.
Fessas, D.
Ragg, E.
Renzetti, S.
Bonomi, F.
Iametti, S.
Publication year
2017
Abstract
Temperature sensitivity of bovine milk beta-lactoglobulin (BLG) was assessed in the presence/absence of non-reducing sugars (sucrose and trehalose) and polyols (glycerol and sorbitol). None of them affected the structural features of the protein at room temperature, where the only observed effect was an increased affinity towards hydrophobic probes in the presence of all co-solutes but glycerol. Although most of the observed effects in temperature-ramp experiments are due to entropic effects (fitting within the “preferential exclusion” theory of protein stabilization), this study indicates that each co-solute exhibit different efficacy at stabilizing specific regions of BLG, suggesting that each of them acts in a specific way on the solvent/protein system. The relevance of these observations with respect to systems of practical relevance is discussed, given the widespread use of heat-polymerizing proteins – such as BLG – in many food formulations that very often include significant amounts of sugars and/or polyols. © 2017 Elsevier Ltd
Subject
Life
FI - Functional Ingredients
ELSS - Earth, Life and Social Sciences
Food and Nutrition
Nutrition
Healthy Living
Polyols
Structure-protecting agents
Temperature-induced unfolding
Entropy
Glycerol
Polyols
Proteins
Stabilization
Sugars
Beta-lactoglobulin
Hydrophobic probes
Presence/absence
Protecting agent
Protein stabilization
Structural feature
Temperature sensitivity
Temperature-induced
Alcohols
To reference this document use:
http://resolver.tudelft.nl/uuid:a500ba1b-870d-43ee-bd3d-9088e0863fe8
DOI
https://doi.org/10.1016/j.foodchem.2017.04.132
TNO identifier
762793
ISSN
0308-8146
Source
Food Chemistry, 234, 155-162
Document type
article