Casein–casein interactions in the presence of dairy associated carbohydrates analysed using surface plasmon resonance
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Casein–casein interactions in the presence of dairy associated carbohydrates analysed using surface plasmon resonance. / De Gobba, Cristian; Møller, Marie S.; Rauh, Valentin; Svensson, Birte; Lund, Marianne N.
In: International Dairy Journal, Vol. 105, 104686, 2020.Research output: Contribution to journal › Journal article › Research › peer-review
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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 -
ID: 240139125