Thermotropic gelation of food proteins

Grinberg, V. Ya.; Grinberg, Natalia V.; Bikbov, T. M.; Bronich, Tatiana K.; Mashkevich, A.Ya.

doi:10.1016/s0268-005x(09)80058-1

Cited by 25 publications

(15 citation statements)

References 50 publications

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“…The rate of these slow relaxation processes corresponds to the rheological behaviour typical of the glassy state and the transition zone from the glassy to the rubber-like state. It is of interest that the rate of these processes is independent of the gel concentration, which controls the gel network density and its modulus of elasticity [31,54,55].…”

Section: Vitrificationmentioning

confidence: 99%

The importance of glassy biopolymer components in food

Tolstoguzov¹

2000

Nahrung

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The glassy state is not just important in low moisture and frozen foods, where it influences the physical and chemical stability and the crispness of some foodstuffs: glassy biopolymer components affect the physical properties of most food systems and low moisture biological systems. Glassy foods are not always fragile and crispy in texture. Therefore, the relationship between mechanical behaviour and molecular dynamics in low-moisture biopolymer systems will be considered. Vitrification of a macromolecular system only requires a mutual fixation of a certain proportion of the chain segments. The higher the rigidity of the chains, the lower the number of the chain segments which must be mutually fixed to vitrify the system. Mechanical stress can help the thermal movement to re-activate the motion of mutually fixed segments and involves a long deformation of glassy material. The stress required to effect long deformation presumably increases up to the strength of the material as the temperature decreases from the glass transition to the temperatures of brittleness (crispness). Vitrification of a loaded viscoelastic system results in an accumulation of mechanical energy (memory effect), which can be released (elastic recovery) above the glass transition temperature due to heating and or addition of a plasticizer. The effects of memory and elastic recovery could be of particular importance for producing foodstuffs which change their form, e.g. self-stirring dry foods and drinks on re-hydration in hot water. The importance of glassy biopolymer ingredients from the viewpoint of food formulation and processing is discussed.

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Section: Vitrificationmentioning

confidence: 99%

The importance of glassy biopolymer components in food

Tolstoguzov¹

2000

Nahrung

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“…Such data reflect that formation of a gel network is subject to kinetic limitations. The equilibrium elasticity modulus (E,, similar to G') of thermotropic protein gels is determined by temperature and time of heating, which can affect kinetic gelling processes, i.e., protein denaturation, diffusion, and hydrolytic destruction (Grinberg et al 1992).…”

Section: Isothermal Heatingmentioning

confidence: 99%

Myofibrillar Protein Gelation: Viscoelastic Changes Related to Heating Procedures

Xiong

Blanchard

1994

Journal of Food Science

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Dynamic rheological properties were investigated during gelation of chicken myofibrillar protein as influenced by heating procedures, Thermal scan (l"C/min) of myofibril suspensions in 0.6M NaCl @H 6.0) induced a major transition in storage modulus (G', peak 48°C) preceded by a transition in protein-protein aggregation (46°C) and accompanied by a marked reduction in actomyosin solubility. Preheating at 50°C diminished the transition and resulted in increased final G' value. Isothermal heating produced complex, temperature-dependent rheological changes'@ and phase angles), particularly within 43-58°C. The rheological transitions of myofibrillar protein were probably related to kinetic changes during formation of elastic gel networks. Such rheological data on gel formation can help predict and control muscle food responses to specific thermal processes.

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“…The gel-forming properties of proteins from soybeans and other legume and oilseed crops have been extensively studied (1)(2)(3)(4)(5)(6)(7). Gill and Tung (8) first demonstrated the ability of a highly glycosylated 12S rapeseed protein to form gels on heating at pH > 4.…”

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Heat‐induced gelation of rapeseed proteins: Effect of protein interaction and acetylation

Schwenke¹,

Dahme²,

Wolter³

1998

J Americ Oil Chem Soc

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The gel-forming abilities of a rapeseed protein isolate, composed of 70% globulin (cruciferin) and 30% albumin (napin), and their individual protein components, were investigated. The influence of acetylation upon the gelation properties was also studied. Highest gel strength (measured as shear modulus) of the isolate was obtained at pH values around 9, which is between the isoelectric points of both major proteins. Purified cruciferin gave the highest shear modulus values, with maxima at pH 6 and 8. Weak and poorly stable gels exhibiting strong hysteresis were obtained with isolated napin. Acetylation resulted in a pH shift of the shear modulus maximum of the protein isolate to about 6. The gelation temperature of the acetylated isolate had the highest pH and concentration dependence compared with the other proteins. JAOCS 75, 83-87 (1998).The ability to form gels is a key functional property in utilizing plant proteins. The gel-forming properties of proteins from soybeans and other legume and oilseed crops have been extensively studied (1-7).Gill and Tung (8) first demonstrated the ability of a highly glycosylated 12S rapeseed protein to form gels on heating at pH > 4. The strongest gels were formed at high pH and ionic strength. The high level of carbohydrate (12.9%) led the authors to assume protein-carbohydrate interaction during gel formation. Thompson et al. (9) observed increased viscosity of a hexametaphosphate-extracted rapeseed protein isolate on heating to 80˚C but did not obtain a gel. Paulson and Tung (10) studied thermally induced gelation of a rapeseed (canola) protein isolate on heating to 72°C. Gels formed only at high pH (>9.5).Léger and Arntfield (11) studied gelation of 12S canola globulin. Gels prepared with 6% protein under alkaline conditions were superior to gels prepared from acidic solutions. The effects of pH, salts, and denaturing and reducing agents on gelation properties led the authors to conclude that hydrophobic forces and electrostatic interactions were responsible for establishing the gel network, while gel stabilization and strengthening were attributed to disulfide bonding, electrostatic interactions, and hydrogen bonding.Succinylation has been used to improve the gel-forming properties of a canola protein isolate by Paulson and Tung (10). In this way, the pH range of gel formation was extended from the alkaline region (pH > 9.5) to 5.0.Comparison of the gel-forming properties of the different rapeseed protein preparations is difficult owing to differences in protein composition and purity. Moreover, data on the protein composition of the isolates studied are scanty.The present paper deals with the influence of the major protein components of rapeseed protein isolate [12S globulin "cruciferin" and 2S protein "napin" (12)] and of acetylation on the gel-forming properties of the isolate. The pH and concentration dependencies on the gelation temperature and the shear modulus of purified cruciferin and napin as well as nonmodified and acetylated isolates containing both proteins...

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Thermotropic gelation of food proteins

Cited by 25 publications

References 50 publications

The importance of glassy biopolymer components in food

The importance of glassy biopolymer components in food

Myofibrillar Protein Gelation: Viscoelastic Changes Related to Heating Procedures

Heat‐induced gelation of rapeseed proteins: Effect of protein interaction and acetylation

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