The Gelation Of Proteins

doi:10.1016/S1043-4526(08)60008-X

Advances in Food and Nutrition Research

Volume 34, 1990, Pages 203-298

https://doi.org/10.1016/S1043-4526(08)60008-X Get rights and content

Publisher Summary

This chapter describes the process of the gelation of proteins. Gelation is a phenomenon; therefore, its definition and that of its product, a gel, is dependent on the perspective of the observer and the technique(s) used to observe it. For example, gels may be defined by their ability to immobilize a liquid, their macromolecular structure, or their textural or rheological properties. The chapter reviews a variety of protein gel systems with a broad perspective stressing similarities between them, yet not without mentioning the important differences that make each unique. It describes the multicomponent protein gels. The rheological and optical properties of thermally irreversible gels are the outcome of two events. First, a change in protein structure is needed that permits protein–protein interactions. The subsequent aggregation process, which is highly influenced by the solvent environment, may produce the gel microstructure, which is responsible for the optical and rheological properties. The physical integrity of a gel is maintained by counterbalancing forces of attraction and repulsion among polymer molecules and between the polymer network and the surrounding solvent

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To enhance the gel properties of PSE (pale, soft, and exudative)-like chicken meat protein isolate (PPI), the effect of peanut, corn, soybean, and sunflower oils on the gel properties of PPI emulsion gels was investigated. Vegetable oils improved emulsion stability and gel strength and enhanced viscosity and elasticity. The gel strength of the PPI–sunflower oil emulsion gel increased by 163.30 %. The thermal denaturation temperature and enthalpy values were increased. They decreased the particle size of PPI emulsion (P < 0.05) and changed the three-dimensional network structure of PPI emulsion gels from reticular to sheet with a smooth surface and pore-reduced lamellar. They elevated the content of immobile water PPI emulsion gels, decreased the α-helix and β-turn, and increased the β-sheet and random coil. Vegetable oil improved the gel properties of PPI in the following order: sunflower oil > soybean oil > corn oil ≈ peanut oil > control group.
Gelatin extraction from chicken skin by conventional and Ohmic heating methods and comparison with commercial halal gelatins
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Gelatin extraction from chicken skins using ohmic heating (OH) is a promising application in the food industry. In this study, the effects of OH parameters (electric field (5, 10, 15, and 20 V/cm) and extraction time (1, 3, and 5 h)) on the extraction yield, physicochemical, functional, rheological, thermal, and microstructural properties of chicken skin gelatin were investigated, as well as comparison with conventional extraction and commercial halal gelatins. Chicken skin gelatins obtained with OH-assisted extraction showed higher ash content resulting in more turbidity than commercial gelatins. OH parameters significantly increased the gelatin yield, and 1 h of OH treatment revealed the highest gel strength amongst the electric field applications, conventional extracted, and bovine gelatin. The melting and gelation temperatures of chicken skin gelatins were higher than bovine gelatin and OH treatment increased the thermal stability. The amino acid composition significantly changed with OH treatment, and total imino acid content, relating to the gelation properties, increased. Functional properties, water and oil binding, emulsifying, and foaming, of chicken skin gelatin were significantly higher than commercial gelatins, and OH treatment significantly increased these properties. Overall, OH extraction of gelatin from chicken skins could be a better option for less extraction time, higher extraction yield, better functionality, and higher thermal stability compared to conventional extraction. It was concluded that chicken skin gelatins extracted using OH have properties that can be an alternative to commercial gelatins, but further purification processes are required.
Evaluating the effect of thermo-reversible and thermo-irreversible curdlan gels on the gelling properties and in vitro digestibility of myofibrillar protein gels under low-salt condition
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The purpose of the present study was to investigate the gelling properties and in vitro digestibility of myofibrillar protein (MP) gels under low-salt condition as mediated by different concentrations of thermo-reversible curdlan gels (TRC) or thermo-irreversible curdlan gels (TIRC). The results showed that the incorporation of TRC or TIRC obviously improved the gel strength and water holding capacity of MP gels (P < 0.05). Those properties were most improved by adding 0.3 % TRC or TIRC with gel strength of 0.18 N or 0.17 N and WHC of 54.85 % or 49.05 %. Meanwhile, both TRC and TIRC promoted the transformation of α-helix into β-sheet, as well as hydrophobic interactions and disulfide bonds, which are the main forces for the maintenance of the MP gels. The microstructure revealed that the formation of dense and uniform protein network structures can be promoted by the addition of TRC or TIRC. The different modes of interaction between TRC or TIRC and MP resulted in different microstructures of the MP gels. Furthermore, incorporation of TRC or TIRC significantly reduced in vitro protein digestibility, especially for the 0.3 % (w/w) form (P < 0.05). Meanwhile, MP gels had the lowest in vitro protein digestibility after the addition of TRC (66.67 %) compared to the form of TIRC (70.93 %). Therefore, our present study indicated that incorporation form of TRC or TIRC have distinct implications on regulating the gelling properties and in vitro digestibility of MP gels under low-salt condition.
Effects and mechanisms of different κ-carrageenan incorporation forms and ionic strength on the physicochemical and gelling properties of myofibrillar protein
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The present work was aimed to investigate the effects of incorporating κ-carrageenan into myofibrillar protein (MP) as a dry powder (CP) or water suspension (CW) and the ionic strength (0.3 or 0.6 M sodium chloride (NaCl)) on MP physicochemical and gelling properties. The results indicated that incorporation of either CP or CW significantly increased turbidity, surface hydrophobicity, particle size and rheological behaviour of MP. In contrast, the protein solubility and fluorescence intensity of MP decreased when added with each form of κ-carrageenan (P < 0.05). These observed effects improved MP's gelling properties and produced a more compact and homogenous gel network after heating treatment. Moreover, the addition of CW rendered higher gel strength, water holding capacity and intermolecular interactions, such as ionic, hydrogen and disulphide bonds and hydrophobic interactions in MP gel compared with those added with CP, especially for 0.3 M NaCl (P < 0.05). Furthermore, addition of CW significantly decreased the α-helix content of MP gels (P < 0.05), which mainly contributing to the transformation from a random structure to an organised configuration. In addition, a higher NaCl concentration (0.6 M) enhanced the gelling properties of MP gels compared with 0.3 M NaCl concentration in the presence of each form of κ-carrageenan. Therefore, our present study indicated that incorporation form of κ-carrageenan and ionic strength have distinctive effects on regulating physicochemical characteristics and improves gelling properties of MP.
Pressure-induced gelation of blended milk and pea protein suspensions
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The pressure-induced (400 MPa for 15 min) gelation of blended skim milk (SMP) and pea protein concentrate (PPC) suspensions (15% w/w) at different ratios (SMP:PPC = 10:0, 8:2, 6:4, 5:5, 4:6, 2:8, 0:10) were studied. Blending milk and pea proteins reduced the gel strength markedly, indicating that milk and pea proteins do not interact with each other to the same extent. The secondary structure of the proteins was not significantly changed after HP treatment. The PPC dominating gels (0:10 and 2:8) had a large increase in surface hydrophobicity indicating higher exposure of hydrophobic clusters. Based on a differential solubility method it was established that the SMP dominating gels are govern mostly by electrostatic and hydrophobic interactions, while disulphide bonds, hydrogen bonds and electrostatic interactions contributed most to the PPC dominating gel networks. The weak 5:5 gel was established solely by hydrophobic interaction between milk and plant proteins. It is suggested that in the milk protein dominant gel (8:2), the milk proteins formed the primary gel structure likely filled with the pea protein secondary gel network and/or aggregates, whereas the inverse occurred in the pea protein dominant gel (2:8). Replacing milk proteins with pea proteins offers a great potential for produce innovative dairy products using high pressure processing, like for example dairy desserts with a neutral pH and textural properties similar to yogurt.
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Understanding the interplay between gluten and wheat starch is crucial for elucidating the digestibility mechanism of gluten in wheat-based products. However, this mechanism remains under-investigated. This study sought to elucidate the influence of starch-induced protein structural modifications on gluten digestion. Our findings revealed that starch considerably enhanced gluten digestion. In the presence of starch, gluten protein digestibility increased from 10.91 % (in the control group with a gluten-to-starch ratio of 1:0) to 14.40 % (in the complex with a gluten-to-corn starch ratio of 1:1). The diminished gluten protein digestibility due to starch may be ascribed to modifications in protein configuration and aggregation behavior. Morphological studies suggested that starch not only functioned as filler particles but also diluted the gluten matrix. A protein network assessment further affirmed that both the junction density and branching rate of gluten proteins decreased notably by 29.9 % and 25.1 %, respectively. Conversely, lacunarity increased by 1.92-fold, compromising the cohesiveness and connectivity of the gluten matrix. Elevated starch concentrations suppressed the formation of disulfide bonds, impeding gluten protein aggregation. Concurrently, gluten-starch interactions were governed by hydrogen bonds and hydrophobic associations. In summary, starch augmented gluten protein digestibility by curtailing their polymerization. This revelation might offer novel perspectives on optimizing gluten protein digestion and utilization.

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^*: Paper No. 8255 in the journal series of the Pennsylvania Agricultural Experiment Station.

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The Gelation Of Proteins*

Publisher Summary

Carbohydr. Polym.

Biochim. Biophys. Acta

Biophys. J.

Int. J. Biol. Macromol.

Polymer

Int. J. Biol. Macromol.

Adv. Protein Chem.

Food Chem.

Food Chem.

Poult. Sci.

Carbohydr. Res.

J. Colloid Interface Sci.

Heat-induced gelation and protein—protein interaction of actomyosin

J. Food Biochem.

Structural characteristics of protein gels as determined by an ultrasound imaging technique

J. Food Sci.

The influence of poultry species, muscle groups, and NaCl level on strength, deformability, and water retention in heat-set muscle gels

J. Food Sci.

Compatibility of gelatin with broad bean globulin in an aqueous medium

J. Food Sci.

Phase equilibria in water–protein–polysaccharide systems II. Water–casein–neutral polysaccharide systems

Colloid Polym. Sci.

Phase equilibria in water–protein–polysaccharide systems III. Water-soy bean globulins–polysaccharide systems

Colloid Polym. Sci.

Liquid two-phase water–protein–polysaccharide systems and their processing into textured protein products

J. Texture Stud.

Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress

Agric. Biol. Chem.

Functionality of muscle proteins in gelation mechanisms of structured meat products

CRC Crit. Rev. Food Sci. Nutr.

Effects of various anions on the rheological and gelling behavior of soy proteins: Thermodynamic observations

J. Agric. Food Chem.

Effect of sample dimensions, lubrication and deformation rate on uniaxial compression of gelatin gels

Rheol. Acta

Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig 1 α-lactalbumin

Biochemistry

Gelling properties of actomyosin from pre- and post-spawning hake (Merluccius hubbsi).

J. Food Sci.

“Muscles, Molecules and Movement.”

Progel and gel formation and reversibility of gelation of whey, soybean, and albumen protein gels

J. Agric. Food Chem.

On the concentration dependence of the elasticity modulus of soybean globulin gels

Polym. Bull.

A study on gelation of soybean globulin solutions 2. Viscoelastic properties and structure of thermotropic gels of soybean globulins

Colloid Polym. Sci.

Thermotropic gelation of proteins

Nahrung

Artifacts and defects of preparation in freeze-etch technique.

The chemistry and biology of collagen.

Preparation of animal tissue for surface-scanning electron microscopy

J. Microsc. (Oxford)

Protein-containing multicomponent gels

Nahrung

Effects of added egg white or whey protein concentrate on thermal transitions in rigidity of croaker surimi

J. Food Sci.

Gelation phenomena of soybean globulins. I. Protein-protein interactions

Cereal Chem.

Thermal aggregation of glycinin subunits

Cereal Chem.

Linear viscoelasticity at the gel point of a crosslinking PDMS with unbalanced stoichiometry

J. Rheol.

Rheology of model polyurethanes at the gel point

Macromolecules

Rheology of soy protein dispersions. Effect of heat and other factors on gelation

Cereal Chem.

The application of network theory to food systems.

Gelation of globular proteins.

The concentration dependence of biopolymer gel modulus

Br. Polym. J.

Electron microscopy of network structures in thermally-induced globular protein gels

Int. J. Pept. Protein Res.

Infrared and laser-raman spectroscopic studies of thermally-induced globular protein gels

Int. J. Pept. Protein Res.

Structure and mechanical properties of agar/bsa co-gels

Prog. Food Nutr. Sci.

Structural and mechanical properties of agar/gelatin co-gels, small deformation studies

Macromolecules

The kinetics of the development of rigidity in gelatin gels

The Gelation Of Proteins^*