Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH

Langton, Maud; Hermansson, Anne‐Marie

doi:10.1016/s0268-005x(09)80122-7

Cited by 386 publications

(313 citation statements)

References 10 publications

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“…4,5 Recently, the assembly of proteins into fibrils has gained more attention in the field of food technology, mainly because of the potential utility in modifying the material properties of food products. Examples of food proteins that have shown the ability to aggregate into fibrils are b-lactoglobulin, bovine serum albumin, lysozyme, and ovalbumin.…”

Section: Introductionmentioning

confidence: 99%

Shear Pulses Nucleate Fibril Aggregation

et al. 2006

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We have studied the effect of shear flow on the formation of amyloid fibrils of the whey protein blactoglobulin. b-Lactoglobulin aggregates into long, thin, and semiflexible fibrils upon heating at low pH and low ionic strength. Solutions with a protein concentration of 0.5% (w/w) were used, and the formation of fibrils was quantified with flow-induced birefringence, a proportional measure of the length concentration of the fibrils. From the decay of the birefringence after cessation of the flow, a length distribution could be fitted. Pulsed and continuous shear treatment of the samples resulted in a comparable enhancement of the fibrillar growth as compared to the fibrillar growth under quiescent conditions. This indicates that the onset of shear flow is the key parameter for the enhancement of fibrillar growth and not the continuous shear flow itself. This behavior is comparable to a nucleation-like process, during which preaggregates of the fibrils are induced during the onset of the flow and orthokinetic coagulation is absent. However, a difference was present in the length distribution between the pulsed and continuously sheared samples, which can be explained by the homogenizing effect of shear flow.

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Section: Introductionmentioning

confidence: 99%

Shear Pulses Nucleate Fibril Aggregation

et al. 2006

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“…These observations lead to the understanding that net charge plays a major role in determining aggregate and gel morphology (Krebs et al, 2009;Langton & Hermansson, 1992). Cryo-EM investigation of aggregates formed from ovalbumin which had been succinylated to various degrees provided further evidence that net charge dominantly determines aggregate morphology (Weijers et al, 2008).…”

Section: Aggregation and Gelationmentioning

confidence: 93%

Application Potential of Food Protein Modification

Jongh¹,

Broersen²

2012

Advances in Chemical Engineering

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“…In the absence of salts, globular proteins often form transparent gels of cross-linked strands (diameter < 10 nm) at a pH higher or lower than pI, the isoelectric point, while forming opaque gels consisting of agglomerated spherical protein particles close to pI [28,29]. β-lactoglobulin (pI = 5.2) adheres to this general picture, forming white particulate gels at pH = 4-6, while forming transparent fine-stranded gels above and below this pH range [30]. It has been shown that close to pI, β-lactoglobulin precipitates out of solution even at room temperature and cannot form stable aggregates reproducibly, while for pH > 5.8 the aggregation process does not depend strongly on pH [28].…”

Section: Introductionmentioning

confidence: 94%

Erratum to: Hydrodynamic dispersion in $ \beta$ -lactoglobulin gels measured by PGSE NMR

et al. 2011

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Abstract. The displacement scale dependent molecular dynamics of solvent water molecules flowing through β-lactoglobulin gels are measured by pulse gradient spin echo (PGSE) nuclear magnetic resonance (NMR). Gels formed under different pH conditions generate structures which are characterized by magnetic resonance imaging (MRI) and PGSE NMR measured dynamics as homogeneous and heterogeneous. The data presented clearly demonstrate the applicability of the theoretical framework for modeling hydrodynamic dispersion to the analysis of protein gels.

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Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH

Cited by 386 publications

References 10 publications

Shear Pulses Nucleate Fibril Aggregation

Shear Pulses Nucleate Fibril Aggregation

Application Potential of Food Protein Modification

Erratum to: Hydrodynamic dispersion in $ \beta$ -lactoglobulin gels measured by PGSE NMR

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