Complexation of β-Lactoglobulin Fibrils and Sulfated Polysaccharides

被引：62

作者：

Jones, Owen G. ^{[1
]}

Handschin, Stephan ^{[1
]}

Adamcik, Jozef ^{[1
]}

Harnau, Ludger ^{[2
,3
]}

Bolisetty, Sreenath ^{[1
]}

Mezzenga, Raffaele ^{[1
]}

机构：

[1] Swiss Fed Inst Technol, Food & Soft Mat Lab, Inst Food Nutr & Hlth, CH-8092 Zurich, Switzerland

[2] Max Planck Inst Intelligente Syst, D-70569 Stuttgart, Germany

[3] Univ Stuttgart, Inst Theoret & Angew Phys, D-70569 Stuttgart, Germany

来源：

BIOMACROMOLECULES | 2011年 / 12卷 / 08期

关键词：

HEAT-INDUCED AGGREGATION; LOW PH; GLOBULAR-PROTEINS; PECTIN COMPLEXES; IONIC-STRENGTH; WHEY PROTEINS; CARRAGEENAN; DENATURATION; COACERVATION; MECHANISM;

D O I：

10.1021/bm200686r

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Fibrils of beta-lactoglobulin, formed by heating at pH 2, were titrated with a sulfated polysaccharide (kappa-carrageenan) to determine the morphology and mechanism of complex formation at low pH. Structural information on the resultant complexes was gathered using transmission electron microscopy, atomic force microscopy, Doppler electrophoresis, and small-angle neutron scattering. Electrophoresis demonstrated that the carrageenan complexed with protein fibrils until reaching a maximum complexation efficiency at a protein/polysaccharide (r) weight ratio of 5:3. Neutron scattering and microscopy indicated an increasing formation of spherical aggregates attached along the protein fibrils with increases in the carrageenan concentration. These globular particles had an average diameter of 30 nm. Small-angle neutron scattering of these complexes could be accurately described by a form factor corresponding to multistranded twisted ribbons with spherical aggregates along their contour length, arranged in a necklace configuration.

引用

页码：3056 / 3065

页数：10

共 63 条

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