Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH β-lactoglobulin gels

Kavanagh, Gaynor M.; Clark, Allan H.; Ross‐Murphy, Simon B.

doi:10.1016/s0141-8130(00)00144-6

Cited by 189 publications

(205 citation statements)

References 26 publications

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“…11 The most common treatment of b-lactoglobulin solutions to induce the formation of fibrils consists of prolonged heating (6-24 h) at 80-C at pH 2 and low ionic strength. 6,[11][12][13][14] The average length of the fibrils depends on the conditions used (e.g., heating time, ionic strength, pH, concentration), but is typically found to be in the range of 1-8 mm. 6,[11][12][13][14] The diameter of the fibrils is around 4 nm, which implies a thickness of 1 or 2 monomers.…”

Section: Introductionmentioning

confidence: 99%

“…6,[11][12][13][14] The average length of the fibrils depends on the conditions used (e.g., heating time, ionic strength, pH, concentration), but is typically found to be in the range of 1-8 mm. 6,[11][12][13][14] The diameter of the fibrils is around 4 nm, which implies a thickness of 1 or 2 monomers. 13 The molecular mechanism of the formation of b-lactoglobulin fibrils is not yet clear.…”

Section: Introductionmentioning

confidence: 99%

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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%

Section: Introductionmentioning

confidence: 99%

Shear Pulses Nucleate Fibril Aggregation

et al. 2006

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“…However, many peptides and proteins, including many globular food proteins that are used as gelling agents, foaming agents or emulsifiers, can also form amyloid-like structures in vitro. Such structures can possess desirable mechanical properties and can be used to create useful textures and structures 12,13 .An example of a fibril formation of globular proteins is provided by the fine-stranded heat-set gels formed by heating solutions of various globular food proteins such as ovalbumin, bovine serum albumin 12 and b-lactoglobulin 13 . b-Lactoglobulin has been particularly well studied, because it represents both a relevant model system and a major whey protein of interest to the food industry [14][15][16][17][18][19][20][21][22] .…”

mentioning

confidence: 99%

mentioning

confidence: 99%

“…An example of a fibril formation of globular proteins is provided by the fine-stranded heat-set gels formed by heating solutions of various globular food proteins such as ovalbumin, bovine serum albumin 12 and b-lactoglobulin 13 . b-Lactoglobulin has been particularly well studied, because it represents both a relevant model system and a major whey protein of interest to the food industry [14][15][16][17][18][19][20][21][22] .…”

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Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

et al. 2010

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The aggregation of proteins is central to many aspects of daily life, including food processing, blood coagulation, eye cataract formation disease and prion-related neurodegenerative infections [1][2][3][4][5] . However, the physical mechanisms responsible for amyloidosis-the irreversible fibril formation of various proteins that is linked to disorders such as Alzheimer's, Creutzfeldt-Jakob and Huntington's diseases-have not yet been fully elucidated [6][7][8][9] . Here, we show that different stages of amyloid aggregation can be examined by performing a statistical polymer physics analysis of single-molecule atomic force microscopy images of heat-denatured b-lactoglobulin fibrils. The atomic force microscopy analysis, supported by theoretical arguments, reveals that the fibrils have a multistranded helical shape with twisted ribbon-like structures. Our results also indicate a possible general model for amyloid fibril assembly and illustrate the potential of this approach for investigating fibrillar systems.Protein self-assembly is a wide-ranging phenomenon and is of great importance in several areas of science. The reversible formation of fibrils from globular proteins is a phenomenon occurring naturally, in vivo, for proteins such as actin and tubulin 10,11 . Other well-known examples of protein fibrillation include the irreversible amyloid fibril formation of various proteins implicated in neurological disorders such as Alzheimer's, Creutzfeldt-Jakob or Huntington's diseases. Typically, these fibrils have long, unbranched, and often twisted structures that are a few nanometres in diameter 1,8 . However, many peptides and proteins, including many globular food proteins that are used as gelling agents, foaming agents or emulsifiers, can also form amyloid-like structures in vitro. Such structures can possess desirable mechanical properties and can be used to create useful textures and structures 12,13 .An example of a fibril formation of globular proteins is provided by the fine-stranded heat-set gels formed by heating solutions of various globular food proteins such as ovalbumin, bovine serum albumin 12 and b-lactoglobulin 13 . b-Lactoglobulin has been particularly well studied, because it represents both a relevant model system and a major whey protein of interest to the food industry [14][15][16][17][18][19][20][21][22] .Despite the fact that the individual parameters controlling the aggregation of globular proteins into amyloid fibrils have been well identified, the driving force for such an aggregation process still remains obscure. Studies devoted to the characterization of fibril structures based on light, neutrons and X-ray scattering methods, being bulk techniques, have only provided an average ensemble picture of the fibrils 23 . Single-molecule techniques such as atomic force microscopy (AFM) and transmission electron microscopy (TEM) have recently emerged to probe amyloid fibrils at the molecular level [24][25][26][27] . Nevertheless, so far, a fully comprehensive picture of the aggregation behaviour...

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Instrumental Techniques for Sample Preparation

Pechak¹,

Smith²

2007

Structure of Dairy Products

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Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH β-lactoglobulin gels

Cited by 189 publications

References 26 publications

Shear Pulses Nucleate Fibril Aggregation

Shear Pulses Nucleate Fibril Aggregation

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

Instrumental Techniques for Sample Preparation

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