Studying a chaperone-like effect of beta-casein on pressure-induced aggregation of beta-lactoglobulin in the presence of alpha-lactalbumin
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Studying a chaperone-like effect of beta-casein on pressure-induced aggregation of beta-lactoglobulin in the presence of alpha-lactalbumin. / Marciniak, Alice; Suwal, Shyam; Brisson, Guillaume; Britten, Michel; Pouliot, Yves; Doyen, Alain.
In: Food Hydrocolloids, Vol. 84, 2018, p. 9-15.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Studying a chaperone-like effect of beta-casein on pressure-induced aggregation of beta-lactoglobulin in the presence of alpha-lactalbumin
AU - Marciniak, Alice
AU - Suwal, Shyam
AU - Brisson, Guillaume
AU - Britten, Michel
AU - Pouliot, Yves
AU - Doyen, Alain
PY - 2018
Y1 - 2018
N2 - Protein aggregation can be used to improve functionality in certain food systems, especially in gelled systems. However, in beverages application, this phenomenon is generally undesirable since it is usually related to protein insolubility and turbidity. Nonetheless, some research has demonstrated a molecular chaperone-like property of certain milk proteins that helps avoid protein aggregation. Here, we investigated the effect of beta-casein (β-CN) on pressure-induced aggregation of beta-lactoglobulin (β-lg) in whey solution using various qualitative and quantitative analyses (turbidity, SDS-PAGE, HPSEC and TEM). Protein model solutions containing different ratios of alpha-lactalbumin (α-la), β-lg and β-CN were pressurized by high hydrostatic pressure (HHP). Pressure treatment of β-lg alone generated a highly turbid solution containing large aggregates while the addition of both proteins (α-la and β-CN) at different ratios led to a drastic decrease in turbidity, despite the presence of larger aggregates. In fact, TEM analysis showed larger and amorphous aggregates for β-lg with α-la and β-CN, and globular, denser aggregates for β-lg alone. Further analysis of these aggregates by fractionation (HPSEC) followed by SDS-PAGE showed no β-CN directly involved in β-lg aggregation, suggesting a chaperone-like effect of β-CN under HHP. Our experiments, performed on model dairy solutions, demonstrated that α-la and β-CN inhibits the formation of insoluble aggregates (decreases turbidity) under HHP treatment of β-lg that could be relevant in milk protein fortified beverages.
AB - Protein aggregation can be used to improve functionality in certain food systems, especially in gelled systems. However, in beverages application, this phenomenon is generally undesirable since it is usually related to protein insolubility and turbidity. Nonetheless, some research has demonstrated a molecular chaperone-like property of certain milk proteins that helps avoid protein aggregation. Here, we investigated the effect of beta-casein (β-CN) on pressure-induced aggregation of beta-lactoglobulin (β-lg) in whey solution using various qualitative and quantitative analyses (turbidity, SDS-PAGE, HPSEC and TEM). Protein model solutions containing different ratios of alpha-lactalbumin (α-la), β-lg and β-CN were pressurized by high hydrostatic pressure (HHP). Pressure treatment of β-lg alone generated a highly turbid solution containing large aggregates while the addition of both proteins (α-la and β-CN) at different ratios led to a drastic decrease in turbidity, despite the presence of larger aggregates. In fact, TEM analysis showed larger and amorphous aggregates for β-lg with α-la and β-CN, and globular, denser aggregates for β-lg alone. Further analysis of these aggregates by fractionation (HPSEC) followed by SDS-PAGE showed no β-CN directly involved in β-lg aggregation, suggesting a chaperone-like effect of β-CN under HHP. Our experiments, performed on model dairy solutions, demonstrated that α-la and β-CN inhibits the formation of insoluble aggregates (decreases turbidity) under HHP treatment of β-lg that could be relevant in milk protein fortified beverages.
KW - Chaperone protein
KW - Dairy proteins
KW - High hydrostatic pressure
U2 - 10.1016/j.foodhyd.2018.05.038
DO - 10.1016/j.foodhyd.2018.05.038
M3 - Journal article
C2 - 10760513
VL - 84
SP - 9
EP - 15
JO - Food Hydrocolloids
JF - Food Hydrocolloids
SN - 0268-005X
ER -
ID: 204113828