Structure and rheology of heat-set gels of globular proteins

Jacques, Laurent; Renard, Denis; Sánchez‐Gimeno, Ana Cristina

doi:10.1007/s003970050121

Cited by 40 publications

(13 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The creep and recovery of cereal doughs are characteristic of a viscoelastic fluid and mostly caused by reorientation of the bonds in viscoelastic material (Onyango and others ). The existence of such irrecoverable strain does not necessarily imply that it is the consequence of flow, but a liquid‐like character (Lefebvre and others ). Sieving showed significant effect on creep and recovery of doughs at a constant shear stress of 30 Pa.…”

Section: Resultsmentioning

confidence: 99%

Oscillatory Rheology and Creep Behavior of Barley β‐d‐glucan Concentrate Dough: Effect of Particle Size, Temperature, and Water Content

Ahmed

Thomas

Ahmadvand

2014

Journal of Food Science

View full text Add to dashboard Cite

Small amplitude oscillatory rheology and creep behavior of β-glucan concentrate (BGC) dough were studied as function of particle size (74, 105, 149, 297, and 595 μm), BGC particle-to-water ratio (1:4, 1:5, and 1:6), and temperature (25, 40, 55, 70, and 85 °C). The color intensity and protein content increased with decreasing particle size by creating more surface areas. The water holding capacity (WHC) and sediment volume fraction increased with increasing particle size from 74 to 595 μm, which directly influences the mechanical rigidity and viscoelasticity of the dough. The dough exhibited predominating solid-like behavior (elastic modulus, G' > viscous modulus, G″). A discrete retardation spectrum is employed to the creep data to obtain retardation time and compliance parameters, which varied significantly with particle size and the process temperature. Creep tests exhibited more pronounced effect on dough behavior compared to oscillatory measurement. The protein denaturation temperature was insignificantly increased with particle fractions from 107 to 110 °C. All those information could be helpful to identify the particle size range and WHC of BGC that could be useful to produce a β-d-glucan enriched designed food.

show abstract

Section: Resultsmentioning

confidence: 99%

Oscillatory Rheology and Creep Behavior of Barley β‐d‐glucan Concentrate Dough: Effect of Particle Size, Temperature, and Water Content

Ahmed

Thomas

Ahmadvand

2014

Journal of Food Science

View full text Add to dashboard Cite

show abstract

“…6, protein molecules randomly associated into large and almost spherical aggregates which then linked together to form the threads of a gel network. We speculated that heat-induced liver protein gel showed 'particulate gel', which was characterised by a kind of opaque coagula (Lefebvre et al, 1998). Gels of the control exhibited a coarse appearance and less homogeneous protein structure.…”

Section: Microstructures Of Gelsmentioning

confidence: 99%

Gelation properties of goose liver protein recovered by isoelectric solubilisation/precipitation process

Li¹,

Xue²,

Zhang³

et al. 2017

Int J of Food Sci Tech

View full text Add to dashboard Cite

Summary Isoelectric solubilisation/precipitation (ISP) process was applied to goose liver (GL) for protein extraction. The gelation properties of proteins extracted by acid processes (ACP, pH 2.0, 2.5 and 3.0) and alkaline processes (ALP, pH 11.0, 11.5 and 12.0) were estimated, where the unextracted ground GL was set as the control. Nearly 58.39~79.00% of GL proteins were recovered by ISP treatments. High molecular weight (100~250 kDa) proteins were found to be partially hydrolysed by ACP, while few changes in proteins occurred during ALP. As evidenced by rheological and textural measurements, ALP proteins formed gels with high elasticity and superior texture, whereas ACP proteins had inferior gelation properties. Moreover, ALP proteins were able to form a highly interconnected and homogeneous three‐dimensional microstructure. Predominantly, gels produced by 11.0 had optimal texture and the lowest cooking loss (P < 0.05). These results suggested that the ISP process (ALP) is a potential method to improve the economic value of GL.

show abstract

“…On the level of the individual BSA molecules constituting these clusters, a 20% increase of their Stokes radii was found upon denaturation. 26 At high NaCl concentrations (2 M), Boye et al observed more pronounced aggregation upon heating. 23 A detailed DSC study on the interplay of denaturation, aggregation and gelation was performed by Barone et al, 27 comparing the behaviors of BSA and its human analog, human serum albumin (HSA).…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, an increase of the gelation temperature with decreasing BSA concentration was observed. The structure formed by thermally denatured BSA solutions was studied by Lefebvre et al 26 via rheology and small-angle neutron scattering. Their results revealed the presence of compact 3D clusters with a smooth surface.…”

Section: Introductionmentioning

confidence: 99%

Evolution of the structure and dynamics of bovine serum albumin induced by thermal denaturation

Matsarskaia

Bühl

Beck

et al. 2020

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

Structure and rheology of heat-set gels of globular proteins

Cited by 40 publications

References 51 publications

Oscillatory Rheology and Creep Behavior of Barley β‐d‐glucan Concentrate Dough: Effect of Particle Size, Temperature, and Water Content

Oscillatory Rheology and Creep Behavior of Barley β‐d‐glucan Concentrate Dough: Effect of Particle Size, Temperature, and Water Content

Gelation properties of goose liver protein recovered by isoelectric solubilisation/precipitation process

Evolution of the structure and dynamics of bovine serum albumin induced by thermal denaturation

Contact Info

Product

Resources

About