Binding interactions between a-glucans from Lactobacillus reuteri and milk proteins characterised by surface plasmon resonance

Silja Kej Diemer; Birte Svensson; Linnéa N. Babol; Darrell Cockburn; Pieter Grijpstra; Lubbert Dijkhuizen; Ditte M.  Folkenberg; Christel Garrigues; Richard Ipsen

doi:10.1007/s11483-012-9260-5

Binding interactions between a-glucans from Lactobacillus reuteri and milk proteins characterised by surface plasmon resonance

Silja Kej Diemer, Birte Svensson, Linnéa N. Babol, Darrell Cockburn, Pieter Grijpstra, Lubbert Dijkhuizen, Ditte M. Folkenberg, Christel Garrigues, Richard Ipsen

9 Citationer (Scopus)

Abstract

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.

Originalsprog	Engelsk
Tidsskrift	Food Biophysics
Vol/bind	7
Udgave nummer	3
Sider (fra-til)	220-226
Antal sider	7
ISSN	1557-1858
DOI	https://doi.org/10.1007/s11483-012-9260-5
Status	Udgivet - sep. 2012

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10.1007/s11483-012-9260-5

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title = "Binding interactions between a-glucans from Lactobacillus reuteri and milk proteins characterised by surface plasmon resonance",

abstract = "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.",

author = "Diemer, {Silja Kej} and Birte Svensson and Babol, {Linn{\'e}a N.} and Darrell Cockburn and Pieter Grijpstra and Lubbert Dijkhuizen and Folkenberg, {Ditte M.} and Christel Garrigues and Richard Ipsen",

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TY - JOUR

T1 - Binding interactions between a-glucans from Lactobacillus reuteri and milk proteins characterised by surface plasmon resonance

AU - Diemer, Silja Kej

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

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.

U2 - 10.1007/s11483-012-9260-5

DO - 10.1007/s11483-012-9260-5

M3 - Journal article

SN - 1557-1858

VL - 7

SP - 220

EP - 226

JO - Food Biophysics

JF - Food Biophysics

IS - 3

ER -

Binding interactions between a-glucans from Lactobacillus reuteri and milk proteins characterised by surface plasmon resonance

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