Large deformation properties of β-lactoglobulin gel structures

Stading, Mats; Hermansson, Anne‐Marie

doi:10.1016/s0268-005x(09)80046-5

Cited by 153 publications

(100 citation statements)

References 9 publications

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“…The increase in failure force, failure stress, and failure strain with increasing WPC concentrations, listed in Table I, was consistent with published results on protein gels. [15][16][17] The effect of pH was found to agree with that reported in the literature. That is, gelation occurred faster at pH 10.0 (t gel ϭ 160 s) than at pH 7.1 (t gel ϭ 210 s) because a high pH is favorable to protein denaturation.…”

Section: Gelation Kinetics and Gel Mechanical Propertiessupporting

confidence: 79%

Whey protein concentrate hydrogels as bioactive carriers

Gunasekaran

Xiao

Eleya

2005

J of Applied Polymer Sci

103

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Two sets of heat-induced hydrogels were prepared from whey protein concentrate (WPC), one set at a constant concentration [15% (w/v)] and varying pHs (pH 5.1-10.0) and the other set at a constant pH (10.0) and varying concentrations (12%, 15%, and 18%). At a given pH, the higher the protein concentration, the shorter was the gelation time and the larger were the equilibrium storage modulus (GЈ ϱ ) and failure stress. For a given protein concentration, the gelation kinetics and mechanical properties of WPC hydrogels were strongly pH dependent. The swelling behavior of WPC gels was studied at 37.5°C Ϯ 0.5°C. The equilibrium swelling ratio (SR) was at the minimum when pH of the swelling medium was close to the isoelectric point (pI) of the whey protein, and when the swelling medium pH was far from the pI (from 6.0 to 10.0), the SR increased. In particular, when the pH was higher than the pI, the swelling was highly pH sensitive. The higher the WPC concentration used in preparing the hydrogel, the lower was the SR. The controlled drug release properties of the WPC hydrogels were studied using caffeine as the model drug. Consistent with the swelling behavior of the gels, release was slower when the pH of the medium was lower (pH 1.8) than when it was higher (pH 7.5). The SR and the drug release rate decreased significantly when the gels were surface-coated with alginate.

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Section: Gelation Kinetics and Gel Mechanical Propertiessupporting

confidence: 79%

Whey protein concentrate hydrogels as bioactive carriers

Gunasekaran

Xiao

Eleya

2005

J of Applied Polymer Sci

103

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“…Heat-induced aggregation proceeds relatively slowly, leading to the formation of a fine-stranded gel structure, composed of finely stranded nanometer thick networks, which are transparent or translucent in appearance and have a rubbery texture (Clark 1998;Ikeda andothers 2000, Ikeda andMorris 2002;Kavanagh and others 2000;Langton and Hermansson 1992;Stading and Hermansson 1991). Intermolecular repulsion can be screened by shifting pH toward the isoelectric point or by increasing the ionic strength.…”

Section: Optical Properties Of Protein Gelationmentioning

confidence: 99%

“…Intermolecular repulsion can be screened by shifting pH toward the isoelectric point or by increasing the ionic strength. These conditions accelerate aggregation via screened conditions and result in the formation of white opaque gel composed of micrometer-sized particulate aggregates (Clark 1998;Langton and Hermansson 1992;Stading and Hermansson 1991;Chantrapornchai and McClements 2002). Electrostatic interactions between protein molecules have a significant influence on the optical properties of globular protein gels.…”

Section: Optical Properties Of Protein Gelationmentioning

confidence: 99%

Influence of Cosolvent Systems on the Gelation Mechanism of Globular Protein: Thermodynamic, Kinetic, and Structural Aspects of Globular Protein Gelation

Baier

McClements

2005

Comp Rev Food Sci Food Safe

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How thermostability and gelation of globular protein are affected by cosolvent systems present in food systems is critical to understanding their functionality. The expression of these functional attributes depends on the molecular structure and thermal‐mechanical history of the protein, as well as its chemical environment. To improve the design of processing protein‐containing food systems, one must fully understand the thermodynamic, kinetic, and structural impact of cosolvent on globular protein gelation. This review focuses on the impact of weakly interacting neutral cosolvent systems (for example, sugars and polyols) on the gelation of globular proteins. The physicochemical mechanisms by which these cosolvent systems can modulate protein gelation are highlighted from a thermodynamic, kinetic, and structural point of view.

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“…Several studies on the physical properties of protein gels and the molecular factors controlling them have been reported, and understanding of the relation between gel microstructure and physical properties has progressed (Arntfield et al, 1990;Stading & Hermansson, 1991;Bottcher & Foegeding, 1994). In addition, the effects of heating temperature and time (Hashizume & Watanabe, 1979;Beveridge et al, 1984;Ker et al, 1993), fatty acid (Yuno-Ohta et al, 1992) and reagents such as NaSCN, Nethylmaleimide and 2-mercaptoethanol (Zheng et al, 1992) on gel formation have also been investigated.…”

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confidence: 99%

Differences in Physical and Structural Properties of Heat-Induced Gels from Glycinins among Soybean Cultivars.

Lee

Matsumoto

Hayashi

et al. 2002

FSTR

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Heat-induced gels were prepared from glycinins of various soybean cultivars at protein concentrations of 18 to 20%. Textural properties of the gels measured by a compression-decompression test were evaluated by the threedimensional representation of the gels through factor analysis of the instrumental data and calculation of factor scores for each gel. Differences in gel texture were clearly observed among the soybean cultivars,with Shirotsurunoko gel being the most fracturable and Yamabe-A3 gel the most unfracturable. The most elastic was the gel from Hill and Matsuura gel exhibited the lowest elasticity. The existence of A4 polypeptide also contributed to the textural features of the gels. The gels of A4-containing cultivars were more unfracturable and less elastic compared to those of A4-lacking cultivars. Physical properties of the gels, gel network structure, and polypeptide composition of the glycinin were related each other to some extent. The compressibility which corresponded to the textural attribute of fracturability was related to regularity and/or pore size of network structure of the gels. The acidic polypeptide of A4 seemed to be responsible for whether the gel network was aggregate or strand type, thereby relating to the physical properties of compressibility and resiliency of the gels. The results obtained here suggest that polypeptide composition of the glycinin affects the properties of gel networks and thereby contributes to different physical and textural properties of the gels.

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Large deformation properties of β-lactoglobulin gel structures

Cited by 153 publications

References 9 publications

Whey protein concentrate hydrogels as bioactive carriers

Whey protein concentrate hydrogels as bioactive carriers

Influence of Cosolvent Systems on the Gelation Mechanism of Globular Protein: Thermodynamic, Kinetic, and Structural Aspects of Globular Protein Gelation

Differences in Physical and Structural Properties of Heat-Induced Gels from Glycinins among Soybean Cultivars.

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