TY - JOUR
T1 - Binding Interactions Between α-glucans from Lactobacillus reuteri and Milk Proteins Characterised by Surface Plasmon Resonance
AU - Diemer, Silja K.
AU - Svensson, Birte
AU - Babol, Linnéa N.
AU - Cockburn, Darrell
AU - Grijpstra, Pieter
AU - Dijkhuizen, Lubbert
AU - Folkenberg, Ditte M.
AU - Garrigues, Christel
AU - Ipsen, Richard H.
N1 - Funding Information:
Acknowledgements The authors would like to thank Danish Agency for Science, Technology and Innovation (FI), Ministry of Science, Technology and Innovation for partly financing the PhD studies of SKD. Darrell Cockburn is a DTU H.C. Ørsted postdoctoral fellow. BS thanks the Danish Council for Independent Research—Natural Sciences (FNU) for funding of the Biacore T100 instrument and a grant for studying protein polysaccharide interactions.
PY - 2012/9
Y1 - 2012/9
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/84865528641
UR - https://www.scopus.com/pages/publications/84865528641#tab=citedBy
U2 - 10.1007/s11483-012-9260-5
DO - 10.1007/s11483-012-9260-5
M3 - Article
AN - SCOPUS:84865528641
SN - 1557-1858
VL - 7
SP - 220
EP - 226
JO - Food Biophysics
JF - Food Biophysics
IS - 3
ER -