TY - JOUR

T1 - Casein–casein interactions in the presence of dairy associated carbohydrates analysed using surface plasmon resonance

AU - De Gobba, Cristian

AU - Møller, Marie S.

AU - Rauh, Valentin

AU - Svensson, Birte

AU - Lund, Marianne N.

PY - 2020

Y1 - 2020

N2 - Ultrahigh temperature (UHT) processed and lactose-free milk are for export to Eastern markets. Free galactose and glucose in lactose-free milk increase occurrence of Maillard products and hence lower milk quality. Notably, enzymatic conversion of galactose into galacto-oligosaccharides (GOS) mitigates such undesirable reactions. As little is known about the effect of GOS on caseins, interactions between caseins in presence or absence of GOS or lactose were assessed by surface plasmon resonance analysis. Based on steady state binding constants (KD) soluble αS-casein showed one order of magnitude lower affinity than soluble β-casein and κ-casein for chip-immobilised αS- and β-casein. By contrast, αS-casein had higher affinity for immobilised κ-casein, followed by β- and κ-casein. The interaction between the caseins did not obey a 1:1 binding model and it was not possible to calculate a precise stoichiometry. Importantly, lactose and GOS exerted very modest or no effect on the various interaction between the caseins.

AB - Ultrahigh temperature (UHT) processed and lactose-free milk are for export to Eastern markets. Free galactose and glucose in lactose-free milk increase occurrence of Maillard products and hence lower milk quality. Notably, enzymatic conversion of galactose into galacto-oligosaccharides (GOS) mitigates such undesirable reactions. As little is known about the effect of GOS on caseins, interactions between caseins in presence or absence of GOS or lactose were assessed by surface plasmon resonance analysis. Based on steady state binding constants (KD) soluble αS-casein showed one order of magnitude lower affinity than soluble β-casein and κ-casein for chip-immobilised αS- and β-casein. By contrast, αS-casein had higher affinity for immobilised κ-casein, followed by β- and κ-casein. The interaction between the caseins did not obey a 1:1 binding model and it was not possible to calculate a precise stoichiometry. Importantly, lactose and GOS exerted very modest or no effect on the various interaction between the caseins.

U2 - 10.1016/j.idairyj.2020.104686

DO - 10.1016/j.idairyj.2020.104686

M3 - Journal article

AN - SCOPUS:85081957695

VL - 105

JO - International Dairy Journal

JF - International Dairy Journal

SN - 0958-6946

M1 - 104686

ER -