表面等离子共振
酪蛋白
化学
罗伊乳杆菌
支化(高分子化学)
葡聚糖
生物化学
生物物理学
乳酸菌
生物
有机化学
发酵
材料科学
纳米技术
纳米颗粒
作者
Silja Kej Diemer,Birte Svensson,Linnéa Nygren Babol,Darrell Cockburn,Pieter Grijpstra,Lubbert Dijkhuizen,Ditte Marie Folkenberg,Christel Garrigues,Richard Ipsen
出处
期刊:Food Biophysics
[Springer Nature]
日期:2012-06-14
卷期号:7 (3): 220-226
被引量:14
标识
DOI:10.1007/s11483-012-9260-5
摘要
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.
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