Journal article
Binding Interactions Between α-glucans from Lactobacillus reuteri and Milk Proteins Characterised by Surface Plasmon Resonance
Interactions between milk proteins and α-glucans at pH 4.0–5.5 were investigated by use of surface plasmon resonance. The α-glucans were synthesised with glucansucrase enzymes from Lactobacillus reuteri strains ATCC-55730, 180, ML1 and 121. Variations in the molecular characteristics of the α-glucans, such as molecular weight, linkage type and degree of branching, influenced the interactions with native and denatured β-lactoglobulin and κ-casein.
The highest overall binding levels were reached with α-(1,4) compared to α-(1,3) linked glucans. Glucans with many α-(1,6) linkages demonstrated the highest binding levels to κ-casein, whereas the interaction with native β-lactoglobulin was suppressed by α-(1,6) linkages. Glucans with a higher degree of branching generally displayed lower protein binding levels whereas a higher molecular weight resulted in increased binding to κ-casein.
The interactions with κ-casein were not pH dependent, whereas binding to denatured β-lactoglobulin was highest at pH 4.0 and binding to native β-lactoglobulin was optimal at pH 4.5–5.0. This study shows that molecular weight, linkage type and degree of branching of α-glucans highly influence the binding interactions with milk proteins.
Language: | English |
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Publisher: | Springer US |
Year: | 2012 |
Pages: | 220-226 |
ISSN: | 15571866 and 15571858 |
Types: | Journal article |
DOI: | 10.1007/s11483-012-9260-5 |
ORCIDs: | Svensson, Birte and 0000-0003-2658-414X |