Effects of a flow field on amyloid fibrillogenesis in a β-lactoglobulin solution

Sharma, Rajesh Kumar; Furusawa, Kazuya; Fukui, Akimasa; Sasaki, Naoki

doi:10.1016/j.ijbiomac.2014.06.034

Cited by 5 publications

(3 citation statements)

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“…Therefore, it seems that mainly the onset of shear flow is important (Akkermans et al., ). Not only the rate of fibril formation, also the morphology of the obtained fibrils is affected by shear flow and the flow regime (Dunstan, Hamilton‐Brown, Asimakis, Ducker, & Bertolini, ; Sharma, Furusawa, Fukui, & Sasaki, ).…”

Section: Bovine Milk Proteinsmentioning

confidence: 99%

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Lambrecht

Jansens

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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Both intrinsic and extrinsic factors impact amyloid formation of food proteins. We here review the impact of various conditions and food constituents on amyloid fibrillation of milk and legume proteins. Much less is known about casein and legume protein amyloid‐like fibril formation than about that of whey proteins such as β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. Proteins of both sources are often studied after heating under strong acidic (pH < 3) conditions. The latter induces changes in protein conformation and often peptide hydrolysis. At higher pH values, alcohols, chaotropic and/or reducing agents induce the conformational changes required to enhance fibrillation. Different types of food proteins can impact each other's fibrillation. Also, the presence of other food constituents can enhance or reduce it. No general conclusions on the mechanisms or impact of different food constituents on food proteins can be made. Optimal conditions for AF formation, that is, heating for several days at low pH, are rare in food processing. However, this does not exclude the possibility of AF formation in food products. For example, slow cooking of hydrolyzed proteins may enhance it. Future research should focus on the prevalence of AFs in complex food systems or model systems relevant for food processing.

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Section: Bovine Milk Proteinsmentioning

confidence: 99%

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Lambrecht

Jansens

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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show abstract

“…Secondary structure of heat-induced fibrillogenesis of β β β β β-lactoglobulin solution at pH 2: Effects of stirring on the heat-induced fibrillogenesis of β-lactoglobulin at pH 2 have been studied in previous study [27] and shown that the fibrillogenesis enhanced with stirring rate but slightly decreased at higher stirring rate due to the fragmentation of fibrils. Rigidrod like fibrils were observed after heating the β-lactoglobulin sample at ≥ 80 °C for 24 h at pH 2 as shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Various techniques have been used earlier to analyze the effect of flow field on the fibrillogenesis of β-lactoglobulin and WPI (whey protein isolate) [24][25][26]. We have analyzed the effect of flow field (stirring) on the fibrillogenesis of β-lactoglobulin at pH 2 [27] and also pH 7 with and without glucose [28] incubated at ≥ 80°C for 24 h. The present work is a continuation of our previous work in which we are characterizing the secondary structure of β-lactoglobulin fibrils by using Fourier transform infrared (FTIR) spectroscopy. Structural study of β-lactoglobulin and its fibrils has been done by many researchers [29].…”

Section: Introductionmentioning

confidence: 99%

FTIR Spectroscopic Study of Heat-Induced β-Lactoglobulin Solution under Flow Field

Sharma¹,

Furusawa²,

Fukui³

et al. 2018

Asian J. Chem.

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Effect of stirring on the secondary structure of amyloid fibrillogenesis of β-lactoglobulin (βLG) at pH 2 and at pH 7 with and without glucose was studied. Fibrillogenesis at pH 2 was carried out by heating the 4w % β-lactoglobulin and at pH 7 by heating the 0.30 mM β-lactoglobulin in 0.1 M, pH 7 sodium phosphate buffer solution with and without glucose (37.5 mM) for 24 h under stirring (250 and 474 rpm) conditions. For control samples, β-lactoglobulin solutions were incubated under unstirred condition at pH 2 and pH 7. The secondary structure of the amyloid fibrils which corresponds the β-sheet structure was studied by using Fourier transform infrared (FTIR) spectroscopy revealed that the stirring does not affect the secondary structure of the β-lactoglobulin fibrils at pH 2 as well as pH 7 with and without glucose.

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Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications

Cao

Mezzenga

2019

Advances in Colloid and Interface Science

367

271

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Effects of a flow field on amyloid fibrillogenesis in a β-lactoglobulin solution

Cited by 5 publications

References 50 publications

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

FTIR Spectroscopic Study of Heat-Induced β-Lactoglobulin Solution under Flow Field

Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications

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